TY - JOUR
T1 - ConSurf 2005
T2 - The projection of evolutionary conservation scores of residues on protein structures
AU - Landau, Meytal
AU - Mayrose, Itay
AU - Rosenberg, Yossi
AU - Glaser, Fabian
AU - Martz, Eric
AU - Pupko, Tal
AU - Ben-Tal, Nir
N1 - Funding Information:
The authors are grateful to the Bioinformatics Unit and the George S. Wise Faculty of Life Sciences at Tel Aviv University for providing technical assistance and computation facilities. This study was supported by a Research Career Development Award from the Israel Cancer Research Fund. T.P. was supported by a grant in Complexity Science from the Yeshaia Horvitz Association and from an ISF grant no. 1208/04. Development of Protein Explorer is supported by a grant to E.M. from the Division of Undergraduate Education of the US National Science Foundation. Funding to pay the Open Access publication charges for this article was provided by Tel Aviv University.
PY - 2005/7
Y1 - 2005/7
N2 - Key amino acid positions that are important for maintaining the 3D structure of a protein and/or its function(s), e.g. catalytic activity, binding to ligand, DNA or other proteins, are often under strong evolutionary constraints. Thus, the biological importance of a residue often correlates with its level of evolutionary conservation within the protein family. ConSurf (http://consurf.tau.ac.il/) is a web-based tool that automatically calculates evolutionary conservation scores and maps them on protein structures via a user-friendly interface. Structurally and functionally important regions in the protein typically appear as patches of evolutionarily conserved residues that are spatially close to each other. We present here version 3.0 of ConSurf. This new version includes an empirical Bayesian method for scoring conservation, which is more accurate than the maximum-likelihood method that was used in the earlier release. Various additional steps in the calculation can now be controlled by a number of advanced options, thus further improving the accuracy of the calculation. Moreover, ConSurf version 3.0 also includes a measure of confidence for the inferred amino acid conservation scores.
AB - Key amino acid positions that are important for maintaining the 3D structure of a protein and/or its function(s), e.g. catalytic activity, binding to ligand, DNA or other proteins, are often under strong evolutionary constraints. Thus, the biological importance of a residue often correlates with its level of evolutionary conservation within the protein family. ConSurf (http://consurf.tau.ac.il/) is a web-based tool that automatically calculates evolutionary conservation scores and maps them on protein structures via a user-friendly interface. Structurally and functionally important regions in the protein typically appear as patches of evolutionarily conserved residues that are spatially close to each other. We present here version 3.0 of ConSurf. This new version includes an empirical Bayesian method for scoring conservation, which is more accurate than the maximum-likelihood method that was used in the earlier release. Various additional steps in the calculation can now be controlled by a number of advanced options, thus further improving the accuracy of the calculation. Moreover, ConSurf version 3.0 also includes a measure of confidence for the inferred amino acid conservation scores.
UR - http://www.scopus.com/inward/record.url?scp=23144448512&partnerID=8YFLogxK
U2 - 10.1093/nar/gki370
DO - 10.1093/nar/gki370
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C2 - 15980475
AN - SCOPUS:23144448512
SN - 0305-1048
VL - 33
SP - W299-W302
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - SUPPL. 2
ER -