Cited by 2,458Protein Structure and DynamicsEnzyme Structure and FunctionRNA and protein synthesis mechanisms

The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.

The relation between the divergence of sequence and structure in proteins.

Open access

Chothia, C., Lesk, A.M.·1986·The EMBO Journal

DOI 10.1002/j.1460-2075.1986.tb04288.xPMC PMC1166865

Open this paper in CoChat — free account

Abstract

Homologous proteins have regions which retain the same general fold and regions where the folds differ. For pairs of distantly related proteins (residue identity approximately 20%), the regions with the same fold may comprise less than half of each molecule. The regions with the same general fold differ in structure by amounts that increase as the amino acid sequences diverge. The root mean square deviation in the positions of the main chain atoms, delta, is related to the fraction of mutated residues, H, by the expression: delta(A) = 0.40 e1.87H.

Integrity signals

Registry

Crossref · 10.1002/j.1460-2075.1986.tb04288.x

Cites

28 of 28 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

The protein data bank: A computer-based archival file for macromolecular structures
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., Rodgers, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · Journal of Molecular Biology · doi:10.1016/s0022-2836(77)80200-3 · Cited by 8,574
The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution
Fermi, G., Perutz, M. F., Shaanan, B., & Fourme, R. (1984) · Journal of Molecular Biology · doi:10.1016/0022-2836(84)90472-8 · Cited by 770
The Protein Data Bank
Bernstein, F. C., Koetzle, T. F., Williams, G. J. B., Meyer, E. F., Brice, M. D., RODGERS, J. R., Kennard, O., Shimanouchi, T., & Tasumi, M. (1977) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1977.tb11885.x · Cited by 763
Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate.
Bolin, J. T., Filman, D. J., Matthews, D. A., Hamlin, R. C., & Kraut, J. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33497-5 · Cited by 746
How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globins
Lesk, A. M., & Chothia, C. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90373-3 · Cited by 712
Self-citation
Structure and refinement of oxymyoglobin at 1·6 Å resolution
Phillips, S. E. V. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90262-4 · Cited by 643
Conformation change of cytochrome c
Takano, T., & Dickerson, R. E. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90529-5 · Cited by 557
Structure of oxidized poplar plastocyanin at 1·6 Å resolution
Guss, J. M., & Freeman, H. C. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80064-3 · Cited by 507
Structure of bovine pancreatic trypsin inhibitor
Wlodawer, A., WALTER, J., Huber, R., & Sjölin, L. (1984) · Journal of Molecular Biology · doi:10.1016/s0022-2836(84)80006-6 · Cited by 478
Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolution
Marquart, M., Deisenhofer, J., Huber, R., & Palm, W. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90252-1 · Cited by 457

Show all 28 references

Sorted by citations

Items 601–700 of 1,005

Molecular replacement then and now
Scapin, G. (2013) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444913011426 · Cited by 61
Molecular recognition of human ephrinB2 cell surface receptor by an emergent African henipavirus
Lee, B., Pernet, O., Ahmed, A. A., Zeltina, A., Beaty, S. M., & Bowden, T. A. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1501690112 · Cited by 63
The PRALINE online server: optimising progressive multiple alignment on the web
Simossis, V. A., & Heringa, J. (2003) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2003.09.002 · Cited by 61
How far can sequences diverge?
Chothia, C., & Gerstein, M. (1997) · Nature · doi:10.1038/385579a0 · Cited by 61
Self-citation
Solution structure of the pleckstrin homology domain of Drosophila β-spectrin
Zhang, P., Talluri, S., Deng, H., Branton, D., & Wagner, G. (1995) · Structure · doi:10.1016/s0969-2126(01)00254-4 · Cited by 61
Common features of the conformations of antigen‐binding loops in immunoglobulins and application to modeling loop conformations
Tramontano, A., & Lesk, A. M. (1992) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340130306 · Cited by 61
Self-citation
Improving protein secondary structure prediction with aligned homologous sequences
Francesco, V. D., Garnier, J., & Munson, P. J. (1996) · Protein Science · doi:10.1002/pro.5560050113 · Cited by 61
Clustering of proximal sequence space for the identification of protein families
Abascal, F., & Valencia, A. (2002) · Bioinformatics · doi:10.1093/bioinformatics/18.7.908 · Cited by 61
Nucleotide sequence and chromosomal location of Cab11 and Cab12, the genes for the fourth polypeptide of the photosystem I light‐harvesting antenna (LHCI)
Schwartz, E., Shen, D., Aebersold, R. H., McGrath, J. M., Pichersky, E., & Green, B. R. (1991) · FEBS Letters · doi:10.1016/0014-5793(91)80299-i · Cited by 61
A Three-Dimensional Model of the Cdc2 Protein Kinase: Localization of Cyclin- and Suc1-Binding Regions and Phosphorylation Sites
Marcote, M. J., Knighton, D. R., Basi, G., Sowadski, J. M., Brambilla, P., Draetta, G. F., & Taylor, S. S. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.8.5122 · Cited by 61
Assessing the utility of CASP14 models for molecular replacement
Millán, C., Keegan, R. M., Pereira, J., Sammito, M. D., Simpkin, A. J., McCoy, A. J., Lupas, A. N., Hartmann, M. D., Rigden, D. J., & Read, R. J. (2021) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26214 · Cited by 62
The role of junctophilin proteins in cellular function
Lehnart, S. E., & Wehrens, X. H. T. (2022) · Physiological Reviews · doi:10.1152/physrev.00024.2021 · Cited by 61
Global and local model quality estimation at CASP8 using the scoring functions QMEAN and QMEANclust
Benkert, P., Tosatto, S. C. E., & Schwede, T. F. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22532 · Cited by 59
Desmosterolosis—phenotypic and molecular characterization of a third case and review of the literature
Schaaf, C. P., Koster, J., Katsonis, P., Kratz, L. E., Shchelochkov, O. A., Scaglia, F., Kelley, R. I., Lichtarge, O., Waterham, H. R., & Shinawi, M. S. (2011) · American Journal of Medical Genetics Part A · doi:10.1002/ajmg.a.34040 · Cited by 60
Three Dimensional Models of Cu 2+ -Aβ(1–16) Complexes from Computational Approaches
Alí‐Torres, J., Maréchal, J., Rodrı́guez-Santiago, L., & Sodupe, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja203407v · Cited by 60
Three-dimensional structure of the HTLV-II matrix protein and comparative analysis of matrix proteins from the different classes of pathogenic human retroviruses
Christensen, A. M., Massiah, M. A., Turner, B. G., Sundquist, W. I., & Summers, M. F. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0700 · Cited by 59
Conformational Variation in Enzyme Catalysis: A Structural Study on Catalytic Residues
Riziotis, I. G., Ribeiro, A. J. M., Borkakoti, N., & Thornton, J. M. (2021) · Journal of Molecular Biology · doi:10.1016/j.jmb.2022.167517 · Cited by 59
Integrated Assessment of Genomic Correlates of Protein Evolutionary Rate
Xia, Y., Franzosa, E. A., & Gerstein, M. (2009) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1000413 · Cited by 59
The RUNX1 Runt Domain at 1.25Å Resolution: A Structural Switch and Specifically Bound Chloride Ions Modulate DNA Binding
Bäckström, S., Wolf‐Watz, M., Grundström, C., Härd, T., Grundström, T., & Sauer, U. H. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00702-7 · Cited by 59
Molecular-docking study of malaria drug target enzyme transketolase in Plasmodium falciparum 3D7 portends the novel approach to its treatment
Hasan, M. A., Mazumder, M. H. H., Chowdhury, A. S., Datta, A., & Khan, M. A. (2015) · Source Code for Biology and Medicine · doi:10.1186/s13029-015-0037-3 · Cited by 63
MICAN : a protein structure alignment algorithm that can handle Multiple-chains, Inverse alignments, C α only models, Alternative alignments, and Non-sequential alignments
Minami, S., Sawada, K., & Chikenji, G. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-24 · Cited by 61
Genomic Determinants of Protein Folding Thermodynamics in Prokaryotic Organisms
Bastolla, U., Moyá, A., Viguera, E., & van Ham, R. C. H. J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.08.086 · Cited by 59
Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building
Adzhubei, A. A., & Sternberg, M. J. E. (1994) · Protein Science · doi:10.1002/pro.5560031223 · Cited by 59
An Automated System for the Analysis of G Protein-Coupled Receptor Transmembrane Binding Pockets: Alignment, Receptor-Based Pharmacophores, and Their Application
Kratochwil, N. A., Malherbe, P., Lindemann, L., Ebeling, M., Hoener, M. C., Mühlemann, A., Porter, R. H. P., Ståhl, M., & Gerber, P. R. (2005) · Journal of Chemical Information and Modeling · doi:10.1021/ci050221u · Cited by 59
Integrative database analysis in structural genomics.
Gerstein, M. (2000) · Nature Structural Biology · doi:10.1038/80739 · Cited by 59
The current state of the art in protein structure prediction
Moult, J. (1996) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(96)80118-2 · Cited by 59
An integrated approach to structural genomics
Heinemann, U., Frevert, J., Hofmann, K., Illing, G., Maurer, C. T. C., Oschkinat, H., & Saenger, W. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00009-2 · Cited by 59
An automated method for modeling proteins on known templates using distance geometry
Srinivasan, S., March, C. J., & Sudarsanam, S. (1993) · Protein Science · doi:10.1002/pro.5560020216 · Cited by 59
Third component of trout complement. cDNA cloning and conservation of functional sites.
Lambris, J. D., Lao, Z., Pang, J., & Alsenz, J. (1993) · The Journal of Immunology · doi:10.4049/jimmunol.151.11.6123 · Cited by 59
Functional inferences from reconstructed evolutionary biology involving rectified databases – an evolutionarily grounded approach to functional genomics
Benner, S. A., Chamberlin, S. G., Liberles, D. A., Govindarajan, S., & Knecht, L. (2000) · Research in Microbiology · doi:10.1016/s0923-2508(00)00123-6 · Cited by 59
A structural role for the PHP domain in E. coli DNA polymerase III
Barros, T. F., Guenther, J. M., Kelch, B. A., Anaya, J., Prabhakar, A., O’Donnell, M. E., Kuriyan, J., & Lamers, M. H. (2013) · BMC Structural Biology · doi:10.1186/1472-6807-13-8 · Cited by 60
Genome and proteome annotation: organization, interpretation and integration
Reeves, G. A., Talavera, D., & Thornton, J. M. (2008) · Journal of The Royal Society Interface · doi:10.1098/rsif.2008.0341 · Cited by 60
Predicting Reliable Regions in Protein Alignments from Sequence Profiles
Tress, M. L., Jones, D. T., & Valencia, A. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00622-3 · Cited by 58
Structural organization of G-protein-coupled receptors
Lomize, A. L., Pogozheva, I. D., & Mosberg, H. I. (1999) · Journal of Computer-Aided Molecular Design · doi:10.1023/a:1008050821744 · Cited by 58
Refined crystal structure of a recombinant immunoglobulin domain and a complementarity-determining region 1-grafted mutant
Steipe, B., Plückthun, A., & Huber, R. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90398-4 · Cited by 58
Insights into drug metabolism by cytochromes P450 from modelling studies of CYP2D6‐drug interactions
Maréchal, J., Kemp, C. A., Roberts, G. C. K., Paine, M. J. I., Wolf, C. R., & Sutcliffe, M. J. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707570 · Cited by 57
Beyond the Twilight Zone: Automated prediction of structural properties of proteins by recursive neural networks and remote homology information
Mooney, C., & Pollastri, G. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22429 · Cited by 57
Insights into the Structural Basis for Zinc Inhibition of the Glycine Receptor
Nevin, S. T., Cromer, B. A., Haddrill, J. L., Morton, C. J., Parker, M. W., & Lynch, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300097200 · Cited by 57
Differential Site Accessibility Mechanistically Explains Subcellular-Specific N-Glycosylation Determinants
Lee, L. Y., Lin, C., Fanayan, S., Packer, N. H., & Thaysen‐Andersen, M. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00404 · Cited by 58
Quantifying the Impact of Protein Tertiary Structure on Molecular Evolution
Choi, S. C., Hobolth, A., Robinson, D. M., Kishino, H., & Thorne, J. L. (2007) · Molecular Biology and Evolution · doi:10.1093/molbev/msm097 · Cited by 60
Crystal structure determination at 1.4 Å resolution of ferredoxin from the green alga Chlorella fusca
Bes, M. T., Parisini, E., Inda, L. A., Saraiva, L. M., Peleato, M. L., & Sheldrick, G. M. (1999) · Structure · doi:10.1016/s0969-2126(00)80054-4 · Cited by 57
Origin of Dimeric Structure in the Ribonuclease Superfamily
Ciglic, M. I., Jackson, P. J., Raillard, S. A., Haugg, M., Jermann, T. M., Opitz, J. G., Trabesinger-Rüf, N., & Benner, S. A. (1998) · Biochemistry · doi:10.1021/bi972203e · Cited by 57
Biochemical characterization and crystalization of human Zn-α 2 -glycoprotein, a soluble class I major histocompatibility complex homolog
Sánchez, L. M., López-Otı́n, C., & Björkman, P. J. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.9.4626 · Cited by 57
A protein structure comparison methodology
Brown, N. P., Orengo, C. A., & Taylor, W. R. (1996) · Computers & Chemistry · doi:10.1016/0097-8485(95)00062-3 · Cited by 57
The 14th barrel rolls out
Chothia, C. (1988) · Nature · doi:10.1038/333598a0 · Cited by 57
Self-citation
Structural adaptation to low temperatures − analysis of the subunit interface of oligomeric psychrophilic enzymes
Tronelli, D., Maugini, E., Bossa, F., & Pascarella, S. (2007) · FEBS Journal · doi:10.1111/j.1742-4658.2007.05988.x · Cited by 56
Structure-based Active Site Profiles for Genome Analysis and Functional Family Subclassification
Cammer, S. A., Hoffman, B. T., Speir, J. A., Canady, M. A., Nelson, M., Knutson, S. T., Gallina, M., Baxter, S. M., & Fetrow, J. S. (2003) · Journal of Molecular Biology · doi:10.1016/j.jmb.2003.09.062 · Cited by 56
Swelfe: a detector of internal repeats in sequences and structures
Abraham, A., Rocha, E. P. C., & Pothier, J. F. (2008) · Bioinformatics · doi:10.1093/bioinformatics/btn234 · Cited by 56
Cytochrome oxidase genes from Thermus thermophilus. Nucleotide sequence of the fused gene and analysis of the deduced primary structures for subunits I and III of cytochrome caa3.
Mather, M. W., Springer, P. A., HENSEL, S., Buse, G., & Fee, J. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53335-4 · Cited by 56
Measurement of the effectiveness of transitive sequence comparison, through a third 'intermediate' sequence.
Gerstein, M. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.8.707 · Cited by 56
New Programs for Protein Tertiary Structure Prediction
Fetrow, J. S., & Bryant, S. H. (1993) · Nature Biotechnology · doi:10.1038/nbt0493-479 · Cited by 55
T-Cell Receptor Cognate Target Prediction Based on Paired α and β Chain Sequence and Structural CDR Loop Similarities
Lanzarotti, E., Marcatili, P., & Nielsen, M. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02080 · Cited by 54
Mapping the glycosyltransferase fold landscape using interpretable deep learning
Taujale, R., Zhou, Z., Yeung, W., Moremen, K. W., Li, S., & Kannan, N. (2021) · Nature Communications · doi:10.1038/s41467-021-25975-9 · Cited by 56
Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures
Li, H., & Poulos, T. L. (1994) · Structure · doi:10.1016/s0969-2126(00)00046-0 · Cited by 55
Cytochromes P450: Their Active-Site Structure and Mechanism of Oxidation
Koymans, L. M. H., den Kelder, G. M. D.-O., Koppele, J. M. T., & Vermeulen, N. P. E. (1993) · Drug Metabolism Reviews · doi:10.3109/03602539308993979 · Cited by 55
Universal Sharing Patterns in Proteomes and Evolution of Protein Fold Architecture and Life
Caetano‐Anollés, G., & Caetano-Anollés, D. (2005) · Journal of Molecular Evolution · doi:10.1007/s00239-004-0221-6 · Cited by 54
The CATH Hierarchy Revisited—Structural Divergence in Domain Superfamilies and the Continuity of Fold Space
Cuff, A. L., Redfern, O., Greene, L. H., Sillitoe, I., Lewis, T. E., Dibley, M., Reid, A. J., Pearl, F. M. G., Dallman, T. J., Todd, A. E., et al. (2009) · Structure · doi:10.1016/j.str.2009.06.015 · Cited by 54
Structural determinants of species‐selective substrate recognition in human and Drosophila serotonin transporters revealed through computational docking studies
Kaufmann, K. W., Dawson, E. S., Henry, L. K., Field, J. R., Blakely, R., & Meiler, J. (2008) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22178 · Cited by 54
On Near-Optimal Alignments of Biological Sequences
Naor, D., & Brutlag, D. L. (1994) · Journal of Computational Biology · doi:10.1089/cmb.1994.1.349 · Cited by 54
On the Relevance of the Met-turn Methionine in Metzincins
Tallant, C., García-Castellanos, R., Baumann, U., & Gomis‐Rüth, F. X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083378 · Cited by 54
Estimation of Inhibitory Effect against Tyrosinase Activity through Homology Modeling and Molecular Docking
Nokinsee, D., Shank, L. P., Lee, V. S., & Nimmanpipug, P. (2015) · Enzyme Research · doi:10.1155/2015/262364 · Cited by 54
Bis-methionyl Coordination in the Crystal Structure of the Heme-binding Domain of the Streptococcal Cell Surface Protein Shp
Aranda, R., Worley, C. E., Liu, M., Bitto, E., Cates, M. S., Olson, J. S., Lei, B., & Phillips, G. N. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.08.058 · Cited by 54
C-terminal domains of Escherichia coli topoisomerase I belong to the zinc-ribbon superfamily
Grishin, N. V. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3841 · Cited by 54
Improving Fold Recognition Without Folds
Przybylski, D., & Rost, B. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.05.041 · Cited by 54
TSP50, a possible protease in human testes, is activated in breast cancer epithelial cells.
Shan, J., Yuan, L., Xiao, Q., Chiorazzi, N., Budman, D. R., Teichberg, S., & Xu, H. (2002) · PubMed · Cited by 54
A Survey of the Primary Structure and the Interspecies Conservation of I-Band Titin's Elastic Elements in Vertebrates
Witt, C. C., Olivieri, N., Centner, T., Kolmerer, B., Millevoi, S., Morell, J., Labeit, D., Labeit, S., Jockusch, H., & Pastore, A. (1998) · Journal of Structural Biology · doi:10.1006/jsbi.1998.3993 · Cited by 53
Recurring structural motifs in proteins with different functions
Orengo, C. A., Flores, T. P., Jones, D. T., Taylor, W. R., & Thornton, J. M. (1993) · Current Biology · doi:10.1016/0960-9822(93)90254-l · Cited by 54
Occurrence of protein structure elements in conserved sequence regions.
Sitbon, E., & Pietrokovski, S. (2007) · BMC Structural Biology · doi:10.1186/1472-6807-7-3 · Cited by 53
Identification of a buried pocket for potent and selective inhibition of Chk1: Prediction and verification
Foloppe, N., Fisher, L. M., Francis, G. L., Howes, R., Kierstan, P., & Potter, A. J. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.10.022 · Cited by 53
Comparative Modeling: The State of the Art and Protein Drug Target Structure Prediction
Liu, T., Tang, G. W., & Capriotti, E. (2011) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/138620711795767811 · Cited by 56
Quantifying the evolutionary divergence of protein structures: The role of function change and function conservation
Pascual‐García, A., Abia, D., Méndez, R., Nido, G. S., & Bastolla, U. (2009) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.22616 · Cited by 51
Structural Similarity between the Prion Domain of HET-s and a Homologue Can Explain Amyloid Cross-Seeding in Spite of Limited Sequence Identity
Wasmer, C., Zimmer, A., Sabaté, R., Soragni, A., Saupe, S. J., Ritter, C., & Meier, B. H. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.06.053 · Cited by 53
A Comparative Study of Modern Homology Modeling Algorithms for Rhodopsin Structure Prediction
Nikolaev, D. M., Shtyrov, A. A., Panov, M. S., Jamal, A., Chakchir, O. B., Kochemirovsky, V. A., Olivucci, M., & Ryazantsev, M. N. (2018) · ACS Omega · doi:10.1021/acsomega.8b00721 · Cited by 53
Computational modeling of RNA 3D structure based on experimental data
Ponce-Salvatierra, A., Astha, A., Merdas, K., Nithin, C., Ghosh, P., Mukherjee, S., & Bujnicki, J. M. (2019) · Bioscience Reports · doi:10.1042/bsr20180430 · Cited by 57
Comparative modelling of human β tubulin isotypes and implications for drug binding
Huzil, J. T., Ludueña, R. F., & Tuszyński, J. A. (2006) · Nanotechnology · doi:10.1088/0957-4484/17/4/014 · Cited by 52
Nucleophilic Participation in the Transition State for Human Thymidine Phosphorylase
Birck, M. R., & Schramm, V. L. (2004) · Journal of the American Chemical Society · doi:10.1021/ja039260h · Cited by 53
Site-Directed Spin-Labeling Study of the Structure and Subunit Interactions along a Conserved Sequence in the α-Crystallin Domain of Heat-Shock Protein 27. Evidence of a Conserved Subunit Interface
Mchaourab, H. S., Berengian, A. R., & Koteiche, H. A. (1997) · Biochemistry · doi:10.1021/bi971700s · Cited by 53
Sugar Specificity of Human .beta.-Cell Glucokinase: Correlation of Molecular Models with Kinetic Measurements
Xu, L. Z., Weber, I. T., Harrison, R. W., Gidh‐Jain, M., & Pilkis, S. J. (1995) · Biochemistry · doi:10.1021/bi00018a011 · Cited by 53
An immunoglobulin-like fold in a major plant allergen: the solution structure of Phl p 2 from timothy grass pollen
Marino, S. D., Morelli, M. A. C., Fraternali, F., Tamborini, E., Musco, G., Vrtala, S., Dolecek, C., Arosio, P., Valenta, R., & Pastore, A. (1999) · Structure · doi:10.1016/s0969-2126(99)80121-x · Cited by 53
Evolution of networks of protein domain organization
Aziz, M. F., & Caetano‐Anollés, G. (2021) · Scientific Reports · doi:10.1038/s41598-021-90498-8 · Cited by 55
The evolutionary dynamics of influenza A virus adaptation to mammalian hosts
Bhatt, S., Lam, T. T., Lycett, S., Brown, A., Bowden, T. A., Holmes, E. C., Guan, Y., Wood, J. L. N., Brown, I. H., Kellam, P., et al. (2013) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2012.0382 · Cited by 53
Structure-based functional identification of a novel heme-binding protein from Thermus thermophilus HB8
Ebihara, A., Okamoto, A., Kousumi, Y., Yamamoto, H., Masui, R., Ueyama, N., Yokoyama, S., & Kuramitsu, S. (2005) · Journal of Structural and Functional Genomics · doi:10.1007/s10969-005-1103-x · Cited by 52
Computational Methods in Drug Design: Modeling G Protein-Coupled Receptor Monomers, Dimers, and Oligomers
Reggio, P. H. (2006) · The AAPS Journal · doi:10.1007/bf02854903 · Cited by 55
Contributions of a Highly Conserved VH/VL Hydrogen Bonding Interaction to scFv Folding Stability and Refolding Efficiency
Tan, P., Sandmaier, B. M., & Stayton, P. S. (1998) · Biophysical Journal · doi:10.1016/s0006-3495(98)74066-4 · Cited by 52
Predicting the helix packing of globular proteins by self‐correcting distance geometry
Mumenthaler, C., & Braun, W. A. (1995) · Protein Science · doi:10.1002/pro.5560040506 · Cited by 50
Structure and function of seed storage proteins in faba bean (Vicia faba L.)
Liu, Y., Wu, X., Hou, W., Li, P., Sha, W., & Tian, Y. (2017) · 3 Biotech · doi:10.1007/s13205-017-0691-z · Cited by 51
3D Flexible Alignment Using 2D Maximum Common Substructure: Dependence of Prediction Accuracy on Target-Reference Chemical Similarity
Kawabata, T., & Nakamura, H. (2014) · Journal of Chemical Information and Modeling · doi:10.1021/ci500006d · Cited by 52
The Nature of Protein Domain Evolution: Shaping the Interaction Network
Bagowski, C. P., Bruins, W., & Velthuis, A. J. W. T. (2010) · Current Genomics · doi:10.2174/138920210791616725 · Cited by 49
Evolutionary innovations and the organization of protein functions in genotype space
Ferrada, E., & Wagner, A. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014172 · Cited by 51
Evolution in action
Scanlan, T. S., & Reid, R. C. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90278-3 · Cited by 51
Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG
Bostina, M., Mohsin, B., Kühlbrandt, W., & Collinson, I. R. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.08.005 · Cited by 50
Relationship between multiple sequence alignments and quality of protein comparative models
Cozzetto, D., & Tramontano, A. L. (2004) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20284 · Cited by 51
Interpreting the Behavior of Enzymes Purpose or Pedigree?
Benner, S. A., & Ellington, A. D. (1988) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238809082549 · Cited by 50
Analysis of six protein structures predicted by comparative modeling techniques
Harrison, R. W., Chatterjee, D., & Weber, I. T. (1995) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340230402 · Cited by 51
The Use of Monoclonal Antibodies and Limited Proteolysis in Elucidation of Structure—Function Relationships in Proteins
Wilson, J. E. (1991) · Methods of biochemical analysis · doi:10.1002/9780470110560.ch4 · Cited by 50
A global view of structure–function relationships in the tautomerase superfamily
Davidson, R., Baas, B., Akiva, E., Holliday, G. L., Polacco, B. J., LeVieux, J. A., Pullara, C. R., Zhang, Y., Whitman, C. P., & Babbitt, P. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.815340 · Cited by 49
The tale of a versatile enzyme: Alpha-amylase evolution, structure, and potential biotechnological applications for the bioremediation of n-alkanes
Pinto, É. S. M., Dorn, M., & Feltes, B. C. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.126202 · Cited by 50
Atomic resolution structures of oxidized [4fe-4s] ferredoxin from Bacillus thermoproteolyticus in two crystal forms: systematic distortion of [4fe-4s] cluster in the protein
Fukuyama, K., Okada, T., Kakuta, Y., & Takahashi, Y. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5292 · Cited by 50
Evolutionary plasticity of protein families: Coupling between sequence and structure variation
Panchenko, A. R., Wolf, Y. I., Panchenko, L. A., & Madej, T. (2005) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.20644 · Cited by 50
The amino acid sequence of glutamate decarboxylase from Escherichia coli
Maras, B., Sweeney, G. E., Barra, D., Bossa, F., & John, R. A. (1992) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1992.tb16609.x · Cited by 50

Authors: Chothia, C., & Lesk, A. M.
ORCID: Lesk, A.M.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1986-04-01
Volume: 5
Issue: 4
Pages: 823-826
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1986.tb04288.x
PMC: PMC1166865
OpenAlex: W1508885706
Cited by: 2,458
References: 28
Citations by year: 2026: 61 · 2025: 56 · 2024: 44 · 2023: 66 · 2022: 62 · 2021: 52 · 2020: 56 · 2019: 59 · 2018: 74 · 2017: 67 · 2016: 64 · 2015: 67 · 2014: 67 · 2013: 100 · 2012: 96
FWCI: 8.63
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM25435)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Keywords: sequence-structure relationship, protein folding, homologous proteins, sequence divergence, structural divergence, RMSD, main-chain conformation, distant homologs
MeSH terms: Amino Acid Sequence, Animals, Humans, Mutation, Protein Conformation, Proteins, Structure-Activity Relationship

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

The relation between the divergence of sequence and structure in proteins.

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks