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Protein Structure Comparison by Alignment of Distance Matrices
Abstract
With a rapidly growing pool of known tertiary structures, the importance of protein structure comparison parallels that of sequence alignment. We have developed a novel algorithm (DALI) for optimal pairwise alignment of protein structures. The three-dimensional co-ordinates of each protein are used to calculate residue-residue (C alpha-C alpha) distance matrices. The distance matrices are first decomposed into elementary contact patterns, e.g. hexapeptide-hexapeptide submatrices. Then, similar contact patterns in the two matrices are paired and combined into larger consistent sets of pairs. A Monte Carlo procedure is used to optimize a similarity score defined in terms of equivalent intramolecular distances. Several alignments are optimized in parallel, leading to simultaneous detection of the best, second-best and so on solutions. The method allows sequence gaps of any length, reversal of chain direction and free topological connectivity of aligned segments. Sequential connectivity can be imposed as an option. The method is fully automatic and identifies structural resemblances and common structural cores accurately and sensitively, even in the presence of geometrical distortions. An all-against-all alignment of over 200 representative protein structures results in an objective classification of known three-dimensional folds in agreement with visual classifications. Unexpected topological similarities of biological interest have been detected, e.g. between the bacterial toxin colicin A and globins, and between the eukaryotic POU-specific DNA-binding domain and the bacterial lambda repressor.
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“The templates were pairwise structurally aligned according to DALILite (41,42), using HIF-2 α as a reference. The sequence alignments were obtained by CLUSTALW (43), and the result was confirmed using the Align-2D command within the MODELLER program (37-39).”
From Structural and Functional Characterization of the Aryl Hydrocarbon Receptor Ligand Binding Domain by Homology Modeling and Mutational Analysis (2007) · cites this paper as [41]
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Computational methods for the structural alignment of molecules
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The PWWP domain of mammalian DNA methyltransferase Dnmt3b defines a new family of DNA-binding folds
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Structure of an Extracellular gp130 Cytokine Receptor Signaling Complex
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“Structural comparisons performed using the DALI (Holm and Sander, 1993) and VAST (Gibrat et al., 1996) servers reveal A B ts reserved a structural homolog of the Cas1 protein.”
MethodDNA polymerase β belongs to an ancient nucleotidyltransferase superfamily
Holm, L. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89071-4 · Cited by 258
Self-citationCrystal Structure of Human DJ-1, a Protein Associated with Early Onset Parkinson's Disease
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Crystal structure of the first three domains of the type-1 insulin-like growth factor receptor
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“Comparison of the L domains with other protein structure”
BackgroundThe FSSP database: fold classification based on structure-structure alignment of proteins
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Self-citationDobbek, H., Gremer, L., Meyer, O. O., & Huber, R. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.16.8884 · Cited by 259
[4] Lipases and hydrolase fold
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“A search of the Dali database (Holm and Sander, 1993) identified several proteins, including bacterial chemotaxis factor CheY (PDB accession code 1Chy) and the energy-coupling IIB enzyme (PDB accession code 1iib-A), which have some similarity to the XRCC1 Cterminal BRCT domain.”
BackgroundMATRAS: a program for protein 3D structure comparison
Kawabata, T. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg581 · Cited by 251
Structural analysis of a set of proteins resulting from a bacterial genomics project
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“1(I)] by the CE search reported here or in an earlier study 46 using Dali, 47 although there are weak similarities to several of the ribosomal proteins, with the CE search giving 1JQM, ribosomal protein L11 as the strongest match.”
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The immunoglobulin fold family: sequence analysis and 3D structure comparisons
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Crystal Structure of a Pumilio Homology Domain
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“The Protein Data Bank was searched for structural neighbors of AfJAMM using the DALI server (Holm and Sander 1993).”
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F‐actin‐like filaments formed by plasmid segregation protein ParM
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“ParM and the actin family of proteins A three-dimensional similarity search (Holm and Sander, 1993) with the structure of ParM revealed MreB and actin as closest relatives (r.”
BackgroundCrystal Structure of the Kelch Domain of Human Keap1
Li, X., Zhang, D., Hannink, M., & Beamer, L. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410073200 · Cited by 256
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“A fold homology search using the DALI server (19) with one of the noncontiguous catalytic domains (ROCs1 via domainswapping; Fig.”
MethodStructural Basis for the Excision Repair of Alkylation-Damaged DNA
Labahn, J., Schärer, O. D., Long, A., Ezaz‐Nikpay, K., Verdine, G. L., & Ellenberger, T. (1996) · Cell · doi:10.1016/s0092-8674(00)80103-8 · Cited by 247
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Molecular architecture of human polycomb repressive complex 2
Ciferri, C., Lander, G. C., Maiolica, A., Herzog, F., Aebersold, R. H., & Nogales, E. (2012) · eLife · doi:10.7554/elife.00005 · Cited by 263
Munc13 C2B domain is an activity-dependent Ca2+ regulator of synaptic exocytosis
Shin, O.-H., Lu, J., Rhee, J.-S., Tomchick, D. R., Pang, Z. P., Wojcik, S. M., Camacho-Perez, M., Brose, N., Machius, M., Rizo, J., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1758 · Cited by 243
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SMG7 Is a 14-3-3-like Adaptor in the Nonsense-Mediated mRNA Decay Pathway
Fukuhara, N., Ebert, J., Unterholzner, L., Lindner, D., Izaurralde, E., & Conti, E. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.01.010 · Cited by 253
RNA Methylation under Heat Shock Control
Bügl, H., Fauman, E. B., Staker, B. L., Zheng, F. F., Kushner, S. R., Saper, M. A., Bardwell, J. C. A., & Jakob, U. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00035-6 · Cited by 241
“identification of four out of seven representative structural homologs (as defined by Dali; Holm and Sander, 1993).”
BackgroundInfluentialHigh‐resolution structure of the E.coli RecQ helicase catalytic core
Bernstein, D. A., Zittel, M. C., & Keck, J. L. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg500 · Cited by 245
Solution Structure of an Arabidopsis WRKY DNA Binding Domain
Yamasaki, K., Kigawa, T., Inoue, M., Tateno, M., Yamasaki, T., Yabuki, T., Aoki, M., Seki, E., Matsuda, T., Tomo, Y., et al. (2005) · The Plant Cell · doi:10.1105/tpc.104.026435 · Cited by 244
“The structures are oriented similarly as aligned by the DALI program (Holm and Sander, 1993), where the aligned segments in (A) and (B) are shown in the same colors used for the corresponding residues of WRKY4-C (C).”
BackgroundMethodInfluentialSolution Structure of a CUE-Ubiquitin Complex Reveals a Conserved Mode of Ubiquitin Binding
Kang, R. S., Daniels, C. M., Francis, S. A., Shih, S. C., Salerno, W. J., Hicke, L., & Radhakrishnan, I. (2003) · Cell · doi:10.1016/s0092-8674(03)00362-3 · Cited by 241
The DNA-binding domain of HIV-1 integrase has an SH3-like fold
Eijkelenboom, A. P. A. M., Lutzke, R. A. P., Boelens, R., Plasterk, R. H. A., Kaptein, R., & Hård, K. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb0995-807 · Cited by 254
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“There will naturally be differences in our and C154, C155 and C165 (Figure 3), which are fully conserved in Btk motifs (Vihinen et al., 1994).structure around the mutated residue R28C compared with the wild-type protein, but these are not thought to be Database searches using the program DALI (Holm and Sander, 1993) h…”
BackgroundXu, T., Sampath, A., Chao, A., Wen, D., Nanao, M., Chêne, P., Vasudevan, S. G., & Lescar, J. (2005) · Journal of Virology · doi:10.1128/jvi.79.16.10278-10288.2005 · Cited by 244
“A search through the Protein Data Bank, using the DALI server (22), did not return any significantly homologous structure, indicating that domain III of Dengue virus NS3 has a unique fold.”
MethodThe structural alignment between two proteins: Is there a unique answer?
Godzik, A. (1996) · Protein Science · doi:10.1002/pro.5560050711 · Cited by 236
“There are, however, a number of algorithms that can produce a reasonable answer (Taylor & Orengo, 1989; Holm & Sander, 1993; Godzik & Skolnick, 1994).”
BackgroundMethodInfluentialToroidal Structure of λ-Exonuclease
Kovall, R. A., & Matthews, B. W. (1997) · Science · doi:10.1126/science.277.5333.1824 · Cited by 241
Structure of the pleckstrin homology domain from β-spectrin
Macías, M. J., Musacchio, A., Ponstingl, H., Nilges, M., Saraste, M., & Oschkinat, H. (1994) · Nature · doi:10.1038/369675a0 · Cited by 239
A comparative analysis of 23 structures of the amyloidogenic protein transthyretin
Hörnberg, A., Eneqvist, T., Olofsson, A., Lundgren, E., & Sauer-Eriksson, A. E. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4078 · Cited by 240
Structure of the haemagglutinin-esterase-fusion glycoprotein of influenza C virus
Rosenthal, P. B., Zhang, X., Formanowski, F., Fitz, W., Wong, C., Meier-Ewert, H., Skehel, J. J., & Wiley, D. C. (1998) · Nature · doi:10.1038/23974 · Cited by 237
“Least-squares superpositions were performed using the program Lsqman 25 .”
MethodCheng, C., Kussie, P. H., Pavletich, N. P., & Shuman, S. (1998) · Cell · doi:10.1016/s0092-8674(00)81411-7 · Cited by 238
Crystal structure of a deubiquitinating enzyme (human UCH‐L3) at 1.8 å resolution
Johnston, S. C., Larsen, C. N., Cook, W. J., Wilkinson, K. D., & Hill, C. P. (1997) · The EMBO Journal · doi:10.1093/emboj/16.13.3787 · Cited by 243
Structure of the TRFH Dimerization Domain of the Human Telomeric Proteins TRF1 and TRF2
Fairall, L., Chapman, L., Moss, H., de Lange, T., & Rhodes, D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00321-5 · Cited by 247
“Of 14DALI (Holm and Sander, 1993) reveal no common topol- ogy.”
Combined sequence and structure analysis of the fungal laccase family
Kumar, S., Phale, P. S., Durani, S., & Wangikar, P. P. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10681 · Cited by 238
“The RMSD calculation (Holm and Sander, 1993) has established that the conformational fold comprising the region 60–70 in the protein is homologous to the conformational fold comprising the region 395–495 in the protein (RMSD value of 1.”
InfluentialCrystal structure of human glyoxalase I—evidence for gene duplication and 3D domain swapping
Cameron, A. D., Olin, B., Ridderström, M., Mannervik, B., & Jones, T. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.12.3386 · Cited by 236
“The Dali program Mildvan,A.S. (1984) X-ray absorption studies of the Zn2 site of (Holm and Sander, 1993) was used to search the FSSP database version glyoxalase I. Biochemistry, 23, 685–689.”
MethodX-Ray Structures of the Universal Translation Initiation Factor IF2/eIF5B
Roll‐Mecak, A., Cao, C., Dever, T. E., & Burley, S. K. (2000) · Cell · doi:10.1016/s0092-8674(00)00181-1 · Cited by 237
“A similarity search using the Dali server (Holm and Sander, 1993) revealed no structural homologs, and we believe that IF2/eIF5B represents a novel protein fold.”
BackgroundMethodInfluentialSearching protein structure databases has come of age
Holm, L., & Sander, C. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190302 · Cited by 236
Self-citationMagni, G., Amici, A., Emanuelli, M., Raffaelli, N., & Ruggieri, S. (1999) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470123195.ch5 · Cited by 235
Characterization of the Structural Features and Interactions of Sclerostin
Veverka, V., Henry, A. J., Slocombe, P. M., Ventom, A. M., Mulloy, B., Muskett, F. W., Muzylak, M., Greenslade, K. J., Moore, A., Zhang, L., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807994200 · Cited by 236
Anantharaman, V., & Aravind, L. (2003) · Genome biology · doi:10.1186/gb-2003-4-12-r81 · Cited by 233
“Searches of the PDB database with query structures was conducted using the DALI program [54].”
MethodRied, M. K., Wild, R., Zhu, J., Pipercevic, J., Sturm, K., Broger, L., Harmel, R. K., Abriata, L. A., Hothorn, L. A., Fiedler, D., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20681-4 · Cited by 239
Structure and mechanism of iron-only hydrogenases
Peters, J. W. (1999) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(99)00028-7 · Cited by 234
Crystal Structure of a GCN5-Related N-acetyltransferase
Wolf, E., Vassilev, A. P., Makino, Y., Šali, A., Nakatani, Y., & Burley, S. K. (1998) · Cell · doi:10.1016/s0092-8674(00)81585-8 · Cited by 233
“The structuresserver (Holm and Sander, 1993) revealed a maximum Z score of 3.3, obtained with a fragment of an unrelated are very similar, with root-mean-square (rms) deviations between a-carbon atomic positions of 0.3 Å, which isa/b protein (b-galactosidase, PDB accession code 1BGLA).”
InfluentialThe Structure of the Human Adenovirus 2 Penton
Zubieta, C., Schoehn, G., Chroboczek, J., & Cusack, S. (2005) · Molecular Cell · doi:10.1016/j.molcel.2004.11.041 · Cited by 244
Saposin fold revealed by the NMR structure of NK-lysin
Liepinsh, E., Andersson, M., Ruysschaert, J., & Otting, G. (1997) · Nature Structural Biology · doi:10.1038/nsb1097-793 · Cited by 231
The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation
Bottomley (2001) · Nature Structural Biology · doi:10.1038/89675 · Cited by 224
“Searches in the Protein Data Bank using the Dali progra”
MethodCluster analysis of molecular conformations
Shenkin, P. S., & McDonald, D. Q. (1994) · Journal of Computational Chemistry · doi:10.1002/jcc.540150811 · Cited by 229
The structural basis of cyclic diguanylate signal transduction by PilZ domains
Benach, J., Swaminathan, S. S., Tamayo, R., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601918 · Cited by 227
TPRpred: a tool for prediction of TPR-, PPR- and SEL1-like repeats from protein sequences
Ranganathappa, M. K., Lupas, A. N., & Söding, J. (2007) · BMC Bioinformatics · doi:10.1186/1471-2105-8-2 · Cited by 226
“) The SCOP classification of MalT as TPR-like is supported both by structural and sequence similarity: (1) A DALI search [19] with the MalT structure [PDB:1HZ4] for structural neighbors yields ten SCOP domains above Z-score of 10, all of them from the TPR family in SCOP (supplementary material, see the file "Additiona…”
BackgroundCrystal Structure of the Dbl and Pleckstrin Homology Domains from the Human Son of Sevenless Protein
Soisson, S. M., Nimnual, A. S., Uy, M., Bar‐Sagi, D., & Kuriyan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81756-0 · Cited by 226
Yan, N., Chai, J., Lee, E. S., et al. (2005) · Nature · doi:10.1038/nature04002 · Cited by 225
Ericsson, D. J., Kasrayan, A., Johansson, P., et al. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.10.079 · Cited by 225
Translation initiation: structures, mechanisms and evolution
Marintchev, A., & Wagner, G. (2004) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583505004026 · Cited by 223
Banfield, M. J., Barker, J. J., Perry, A. C. F., et al. (1998) · Structure · doi:10.1016/s0969-2126(98)00125-7 · Cited by 225
Cai, M., Huang, Y., Ghirlando, R., Wilson, K. L., Craigie, R., & Clore, G. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.16.4399 · Cited by 234
“A search of the DALI structural database (Holm and Sander, 1993) indicates the existence of structurally homologous domains in a number of DNA and RNA binding proteins.”
Станиславович, М. Л., Bhagat, S., Brunning, A., Campbell, E. A., Darst, S. A., Ebright, R. H., & Severinov, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.3.892 · Cited by 226
Parser for protein folding units
Holm, L., & Sander, C. (1994) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340190309 · Cited by 230
“Experiment shows that all the regions that fold early interact extensively with the P-~heet.~~ (2) The first cut in the tree decomposition of apomyoglobin [(l-19 + 71-153)( 20-70 ))] splits open the haem pocket.”
BackgroundInfluentialSelf-citationSensor domains of two-component regulatory systems
Cheung, J., & Hendrickson, W. A. (2010) · Current Opinion in Microbiology · doi:10.1016/j.mib.2010.01.016 · Cited by 224
“Cytoplasmic sensors FixL PAS [31 ,32–37,38 ,39] MmoS PAS [42] DosS GAF [47] DosT GAF [48] DevS GAF [49] BphP–PCD PAS, GAF, PHY [50,51 ,52–54] server [45] detect greater similarities between various PDC sensors with each other than with other PAS sensors.”
SCA3: Neurological features, pathogenesis and animal models
Rieß, O., Rüb, U., Pastore, A., Bauer, P., & Schöls, L. J. (2008) · The Cerebellum · doi:10.1007/s12311-008-0013-4 · Cited by 227
“The two closest matches according to DALI ( 109 ) are the crystal structures of staphopain from S. aureus (110) and the Pseudomonas avirulence protease AVRPPH3 (111), even though the overall sequence identities with these two proteins are well below the level regarded as significant (16% and 11%).”
BackgroundLawrence, M. C., Pilling, P. A., Epa, V. C., Berry, A. M., Ogunniyi, A. D., & Paton, J. C. (1998) · Structure · doi:10.1016/s0969-2126(98)00153-1 · Cited by 224
“The structure of PsaA was compared to those in the Brookhaven Protein Data Bank (PDB) by submitting the Cα coordinates of PsaA to the DALI server [15].”
MethodGerstein, M., & Levitt, M. (1998) · Protein Science · doi:10.1002/pro.5560070226 · Cited by 221
“…& Matthews, 1980; Satow et al., 1987; Artymiuk et al., 1989; Taylor & Orengo, 1989; Sali & Blundell, 1990; Vriend et al., 1991; Russell & Barton, 1992; Grindley et al., 1993; Holm & Sander, 1993a; Godzik & Skolnick, 1994; Feng & Sippl, 1996; Falicov & Cohen, 1996; Gibrat et al., 1996; Cohen, 1997).”
BackgroundMethodInfluentialTeriete, P., Banerji, S., Noble, M. E. M., Blundell, C. D., Wright, A. J., Pickford, A. R., Lowe, E. D., Mahoney, D. J., Tammi, M., Kahmann, J. D., et al. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00080-2 · Cited by 222
Liemann, S., Chandran, K., Baker, T. S., Nibert, M. L., & Harrison, S. C. (2002) · Cell · doi:10.1016/s0092-8674(02)00612-8 · Cited by 226
“Comparison, using the DALI algorithm (Holm and Sander, 1993), of domains I–III with all threedimensional protein structures in the Protein Data Bank reveals no closely related protein fold.”
Protein function annotation by homology-based inference
Loewenstein, Y., Raimondo, D., Redfern, O., Watson, J., Frishman, D., Michal Linial, B., Orengo, C. A., Thornton, J. M., & Tramontano, A. L. (2009) · Genome biology · doi:10.1186/gb-2009-10-2-207 · Cited by 221
“Although not directly coupled to a curated domainfamily resource such as CATH and SCOP, other global structure-comparison methods (for example, DALI [33], MSDFold [34], VAST [35], CE [36], STRUCTAL [37] and FATCAT [38]) can identify structural neighbors in the Protein Data Bank (PDB) [39] (see Box 1), which may share…”
MethodHollis, T., Ichikawa, Y., & Ellenberger, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.4.758 · Cited by 222
“The sequences of AlkA, MutY and Endo III are aligned based on the best superposition of Cα atoms in the crystal structures, as determined by the program DALI (Holm and Sander, 1993).”
MethodReuter, K., Mofid, M. R., Marahiel, M. A., & Ficner, R. (1999) · The EMBO Journal · doi:10.1093/emboj/18.23.6823 · Cited by 221
“program DALI (Holm and Sander, 1993) did not reveal a protein structure with significant similarity to Sfp.”
BackgroundMethodTwo independent routes of de novo vitamin B6 biosynthesis: not that different after all
Fitzpatrick, T. B., Amrhein, N., Kappes, B., Macheroux, P., Tews, I., & Raschle, T. (2007) · Biochemical Journal · doi:10.1042/bj20070765 · Cited by 221
Guasch, A., Pous, J., Ibarra, B., Gomis‐Rüth, F. X., Valpuesta, J., de Sousa, N. C., Carrascosa, J. L., & Coll, M. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5278 · Cited by 223
Parris, K. D., Lin, L., Tam, A., Mathew, R. S., Hixon, J., Stahl, M., Fritz, C., Seehra, J. S., & Somers, W. S. (2000) · Structure · doi:10.1016/s0969-2126(00)00178-7 · Cited by 217
Artus, C., Boujrad, H., Bouharrour, A., Brunelle-Navas, M.-N., Hoos, S., Yuste, V. J., Lenormand, P., Rousselle, J.-C., Namane, A., England, P., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.43 · Cited by 230
“H2AX structure was modelled from NCP with DALI (Holm and Sander, 1993).”
MethodFranco, O. L., Rigden, D. J., Melo, F. R., Bloch, C., Silva, C. P., & Grossi‐de‐Sá, M. F. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01199.x · Cited by 221
Kemmink, J., Darby, N. J., Dijkstra, K., et al. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00119-9 · Cited by 220
Chen, L., Gorman, J. J., McKimm‐Breschkin, J. L., Lawrence, L. J., Tulloch, P. A., Smith, B. J., Colman, P. M., & Lawrence, M. C. (2001) · Structure · doi:10.1016/s0969-2126(01)00581-0 · Cited by 222
Chen, Y. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00086-1 · Cited by 219
“The N-terminal domain, residues 2–107, is structurally unrelated to the N-terminal domains of other family members, and we found no significant structural homologs for it in the protein data bank using the Dali webserver (Holm and Sander, 1993).”
BackgroundPlacement of the Structural Proteins in Sindbis Virus
Zhang, W., Mukhopadhyay, S., Pletnev, S. V., Baker, T. S., Kuhn, R. J., & Rossmann, M. G. (2002) · Journal of Virology · doi:10.1128/jvi.76.22.11645-11658.2002 · Cited by 218
“A rough scale of similarity can be established by measuring the number and percentage of C atoms that can be sequentially aligned in three dimensions (22, 31, 56).”
BackgroundDaniels, D. S., Mol, C. D., Arvai, A. S., Kanugula, S., Pegg, A. E., & Tainer, J. A. (2000) · The EMBO Journal · doi:10.1093/emboj/19.7.1719 · Cited by 219
“Structurally implicated DNA-binding mode To elucidate the manner in which AGT binds DNA, we used the DALI structural comparison algorithm (Holm and Sander, 1993) to search for DNA-binding proteins with homology to AGT.”
MethodA Conserved HEAT Domain within eIF4G Directs Assembly of the Translation Initiation Machinery
Marcotrigiano, J., Lomakin, I. B., Sonenberg, N., Pestova, T. V., Hellen, C. U. T., & Burley, S. K. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00167-8 · Cited by 223
Chowdhury, S., Carter, J. J., Rollins, M. F., Golden, S. M., Jackson, R. N., Hoffmann, C., Nosaka, L., Bondy‐Denomy, J., Maxwell, K. L., Davidson, A. R., et al. (2017) · Cell · doi:10.1016/j.cell.2017.03.012 · Cited by 216
“(C) The Cas8f structurewas used to perform structural homology search usingDali (Holm and Sander, 1993).”
BackgroundMethodInfluentialCrystal structure and biochemical analyses reveal Beclin 1 as a novel membrane binding protein
Huang, W., Choi, W.-Y., Hu, W., Mi, N., Guo, Q., Ma, M., Liu, M., Tian, Y., Lu, P., Wang, F., et al. (2012) · Cell Research · doi:10.1038/cr.2012.24 · Cited by 223
An NMR approach to structural proteomics
Yee, A. A., Chang, X., Pineda‐Lucena, A., Wu, B., Semesi, A., Le, B., Ramelot, T. A., Lee, G., Bhattacharyya, S., Gutierrez, P., et al. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.042684599 · Cited by 217
Hatherley, D., Graham, S. C., Turner, J., Harlos, K., Stuart, D. I., & Barclay, A. N. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.026 · Cited by 216
Li, L., Liu, X., Yang, W., Feng, X., Wang, W., Feng, L., Bartlam, M. G., Wang, L., & Rao, Z. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.11.069 · Cited by 217
Structure of the catalytic domain of the hepatitis C virus NS2-3 protease
Lorenz, I. C., Marcotrigiano, J., Dentzer, T. G., et al. (2006) · Nature · doi:10.1038/nature04975 · Cited by 215
Metadata
- Authors
- Holm, L., & Sander, C.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Venue
- Journal of Molecular Biology
- Publisher
- Elsevier BV
- Published
- 1993-09
- Volume
- 233
- Issue
- 1
- Pages
- 123-138
- ISSN
- 0022-2836 (ISSN-L)
- OpenAlex
- W2022058405
- Cited by
- 3,984
- References
- 0
- Citations by year
- 2026: 23 · 2025: 31 · 2024: 22 · 2023: 22 · 2022: 28 · 2021: 27 · 2020: 53 · 2019: 50 · 2018: 45 · 2017: 42 · 2016: 53 · 2015: 65 · 2014: 73 · 2013: 106 · 2012: 98
- FWCI
- 15.32
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- 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 › Genomics and Phylogenetic Studies
- Keywords
- protein structure comparison, Dali, Monte Carlo optimization, structural similarity, protein fold classification, structural core, colicin A, globin, lambda repressor, sequence gaps
- MeSH terms
- Actins, Algorithms, Amino Acid Sequence, Colicins, DNA-Binding Proteins, Globins, Heat-Shock Proteins, Hexokinase, Models, Molecular, Molecular Sequence Data, Monte Carlo Method, Muramidase, Software, Reproducibility of Results, Cluster Analysis, Sequence Alignment, Sequence Homology, Amino Acid, Protein Structure, Secondary, Protein Structure, Tertiary
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