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

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Abstract

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.

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Brannetti, B., & Helmer-Citterich, M. (2003). iSPOT: A web tool to infer the interaction specificity of families of protein modules. Nucleic Acids Research, 31(13), 3709–3711. https://doi.org/10.1093/nar/gkg592

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