ConSurf 2005: The projection of evolutionary conservation scores of residues on protein structures

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

ABSTRACT 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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Available from: Nir Ben-Tal, Sep 26, 2015
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    • "Using ConSurf [21], we found that regions of high sequence conservation are mainly located at the subunit interfaces (Fig. 5a), supporting the physiological nature of the observed hexamer. However, the two salt bridges that stabilize adjacent monomers in E. coli are not conserved. "
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    • ": Sahillioglu et al., Structural and Dynamics Aspects of ASC Speck Assembly, Structure (2014), 10 . 1016/j.str.2014.09.011 motion of PYD ( Figure 3 ) , which will be discussed . On the other hand , mutations G65A , R74A , L181A , and R182A did not affect the speck formation . G65 and K181 are among highly conserved amino acids ( Landau et al . , 2005 ) . L181A and R182A may relate another functional site . Alanine is yet observed at positions G65 and R74 within the ASC homologs ' structures and thus another substitution might show an effect . On the other hand , the R74 corresponding position on pyrin PYD ( R75A ) was shown to disrupt the pyrin PYD - ASC PYD association ( Vajjhala e"
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