iSPOT: a web tool to infer the interaction specificity of families of protein modules

被引:27
作者
Brannetti, B [1 ]
Helmer-Citterich, M [1 ]
机构
[1] Univ Roma Tor Vergata, Dept Biol, Ctr Mol Bioinformat, I-00133 Rome, Italy
关键词
D O I
10.1093/nar/gkg592
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
iSPOT (http://cbm.bio.uniroma2.it/ispot) is a web tool developed to infer the recognition specificity of protein module families; it is based on the SPOT procedure that utilizes information from position-specific contacts, derived from the available domain/ligand complexes of known structure, and experimental interaction data to build a database of residue-residue contact frequencies. iSPOT is available to infer the interaction specificity of PDZ, SH3 and WW domains. For each family of protein domains, iSPOT evaluates the probability of interaction between a query domain of the specified families and an input protein/peptide sequence and makes it possible to search for potential binding partners of a given domain within the SWISS-PROT database. The experimentally derived interaction data utilized to build the PDZ, SH3 and WW databases of residue-residue contact frequencies are also accessible. Here we describe the application to the WW family of protein modules.
引用
收藏
页码:3709 / 3711
页数:3
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