ConSurf 2010: calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
Top Cited Papers
Open Access
- 15 May 2010
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 38 (Web Server), W529-W533
- https://doi.org/10.1093/nar/gkq399
Abstract
It is informative to detect highly conserved positions in proteins and nucleic acid sequence/structure since they are often indicative of structural and/or functional importance. ConSurf (http://consurf.tau.ac.il) and ConSeq (http://conseq.tau.ac.il) are two well-established web servers for calculating the evolutionary conservation of amino acid positions in proteins using an empirical Bayesian inference, starting from protein structure and sequence, respectively. Here, we present the new version of the ConSurf web server that combines the two independent servers, providing an easier and more intuitive step-by-step interface, while offering the user more flexibility during the process. In addition, the new version of ConSurf calculates the evolutionary rates for nucleic acid sequences. The new version is freely available at: http://consurf.tau.ac.il/.Keywords
This publication has 36 references indexed in Scilit:
- The ConSurf-DB: pre-calculated evolutionary conservation profiles of protein structuresNucleic Acids Research, 2008
- The Universal Protein Resource (UniProt)Nucleic Acids Research, 2007
- Protein database searches using compositionally adjusted substitution matricesThe FEBS Journal, 2005
- ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structuresNucleic Acids Research, 2005
- ConSurf: Identification of Functional Regions in Proteins by Surface-Mapping of Phylogenetic InformationBioinformatics, 2003
- Rate4Site: an algorithmic tool for the identification of functional regions in proteins by surface mapping of evolutionary determinants within their homologuesBioinformatics, 2002
- A General Empirical Model of Protein Evolution Derived from Multiple Protein Families Using a Maximum-Likelihood ApproachMolecular Biology and Evolution, 2001
- The Protein Data BankNucleic Acids Research, 2000
- Twilight zone of protein sequence alignmentsProtein Engineering, Design and Selection, 1999
- Estimation of the number of nucleotide substitutions when there are strong transition-transversion and G+C-content biases.Molecular Biology and Evolution, 1992