ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures.
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.
Landau
Meytal
M
Department of Biochemistry, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 69978, Israel.
Mayrose
Itay
I
Rosenberg
Yossi
Y
Glaser
Fabian
F
Martz
Eric
E
Pupko
Tal
T
Ben-Tal
Nir
N
D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry; D001499:Bayes Theorem; D019143:Evolution, Molecular; D020407:Internet; D008958:Models, Molecular; D015221:Potassium Channels / Q000737:chemistry; D011487:Protein Conformation; D012984:Software
D000596:Amino Acids; D001426:Bacterial Proteins; D015221:Potassium Channels; C107790:prokaryotic potassium channel