Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, Pupko T et al. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 33(Web Server issue): W299-W302

Department of Cell Research and Immunology, Tel Aviv University, Tell Afif, Tel Aviv, Israel
Nucleic Acids Research (Impact Factor: 9.11). 08/2005; 33(Web Server issue):W299-302. DOI: 10.1093/nar/gki370
Source: PubMed


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 ( 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.

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