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 accessAbstract
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.
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“The two most critical issues in homology modeling are the degree of similarity between the target sequence and the templates and the reliability of the alignment, two aspects that are intrinsically interconnected (60).”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [60]
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Cites
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
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
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
Lesk, A. M., & Chothia, C. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90373-3 · Cited by 712
Self-citationStructure 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
Marquart, M., Deisenhofer, J., Huber, R., & Palm, W. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90252-1 · Cited by 457
Structure of erythrocruorin in different ligand states refined at 1·4 Å resolution
Steigemann, W., & Weber, E. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90332-2 · Cited by 301
Artymiuk, P. J., & Blake, C. C. F. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90125-x · Cited by 289
Comparative model-building of the mammalian serine proteases
Greer, J. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90465-4 · Cited by 289
Structure of actinidin, after refinement at 1.7 Å resolution
Baker, E. N. (1980) · Journal of Molecular Biology · doi:10.1016/0022-2836(80)90255-7 · Cited by 287
Evolution of proteins formed by β-sheets
Lesk, A. M., & Chothia, C. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90179-6 · Cited by 272
Self-citationKamphuis, I. G., Drenth, J. P. H., & Baker, E. N. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90348-1 · Cited by 272
Matsuura, Y., Takano, T., & Dickerson, R. E. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90335-7 · Cited by 259
Read, R. J., Fujinaga, M., Sielecki, A. R., & James, M. N. G. (1983) · Biochemistry · doi:10.1021/bi00288a012 · Cited by 195
Refined crystal structure of γ-chymotrypsin at 1.9 Å resolution
Cohen, G. H., Silverton, E. W., & Davies, D. R. (1981) · Journal of Molecular Biology · doi:10.1016/0022-2836(81)90186-8 · Cited by 142
Woodbury, R. G., Katunuma, N., Kobayashi, K., Titani, K., Neurath, H., Anderson, W. F., & Matthews, B. W. (1978) · Biochemistry · doi:10.1021/bi00598a010 · Cited by 139
Structure of azurin from Alcaligenes denitrificans at 2·5 Å resolution
Norris, G. E., Anderson, B. F., & Baker, E. N. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80216-2 · Cited by 137
Pseudomonas cytochrome c551 at 2.0 A resolution: enlargement of the cytochrome c family.
Almassy, R. J., & Dickerson, R. E. (1978) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.75.6.2674 · Cited by 137
Structure of rice ferricytochrome c at 2·0 Å resolution
Ochi, H., Hata, Y., Tanaka, N., Kakudo, M., Sakurai, T., Aihara, S., Morita, Y., & Huber, R. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80092-8 · Cited by 130
Evolution of proteins formed by β-sheets
Chothia, C., & Lesk, A. M. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90178-4 · Cited by 128
Self-citationStructure of a novel bence-jones protein (Rhe) fragment at 1·6 Å resolution
Furey, W. S., Wang, B. C., Yoo, C. S., Sax, M., & Huber, R. (1983) · Journal of Molecular Biology · doi:10.1016/s0022-2836(83)80104-1 · Cited by 117
Protein structure refinement: Streptomyces griseus serine protease A at 1.8 Å resolution
Sielecki, A. R., Hendrickson, W. A., Broughton, C. G., Delbaere, L. T. J., Brayer, G. D., & James, M. N. G. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90486-8 · Cited by 105
Critical evaluation of comparative model building of Streptomyces griseus trypsin
Read, R. J., Brayer, G. D., Jurášek, L., & James, M. N. G. (1984) · Biochemistry · doi:10.1021/bi00321a045 · Cited by 81
Chothia, C., & Lesk, A. M. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90033-6 · Cited by 65
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SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modeling
Guex, N., & Peitsch, M. C. (1997) · Electrophoresis · doi:10.1002/elps.1150181505 · Cited by 11,297
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Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040
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Metadata
- Authors
- Chothia, C., & Lesk, A. M.
- ORCID
- Lesk, A.M.
- Venue
- The EMBO Journal
- Published
- 1986-04-01
- Volume
- 5
- Issue
- 4
- Pages
- 823-826
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- 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
- 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
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