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.

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 [10.1093/nar/gkg592].

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

HELMER CITTERICH, MANUELA
2003-07-01

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.
1-lug-2003
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore BIO/11 - BIOLOGIA MOLECOLARE
English
Con Impact Factor ISI
Protein Structure, Tertiary; src Homology Domains; Sequence Analysis, Protein; Proteins; Databases, Protein; Software; Internet; Ligands; Binding Sites
http://nar.oxfordjournals.org/content/31/13/3709.full
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 [10.1093/nar/gkg592].
Brannetti, B; HELMER CITTERICH, M
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2108/14890
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