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A database for G proteins and their interaction with GPCRs

BACKGROUND: G protein-coupled receptors (GPCRs) transduce signals from extracellular space into the cell, through their interaction with G proteins, which act as switches forming hetero-trimers composed of different subunits (α,β,γ). The α subunit of the G protein is responsible for the recognition...

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Autores principales: Elefsinioti, Antigoni L, Bagos, Pantelis G, Spyropoulos, Ioannis C, Hamodrakas, Stavros J
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2004
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC544346/
https://www.ncbi.nlm.nih.gov/pubmed/15619328
http://dx.doi.org/10.1186/1471-2105-5-208
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author Elefsinioti, Antigoni L
Bagos, Pantelis G
Spyropoulos, Ioannis C
Hamodrakas, Stavros J
author_facet Elefsinioti, Antigoni L
Bagos, Pantelis G
Spyropoulos, Ioannis C
Hamodrakas, Stavros J
author_sort Elefsinioti, Antigoni L
collection PubMed
description BACKGROUND: G protein-coupled receptors (GPCRs) transduce signals from extracellular space into the cell, through their interaction with G proteins, which act as switches forming hetero-trimers composed of different subunits (α,β,γ). The α subunit of the G protein is responsible for the recognition of a given GPCR. Whereas specialised resources for GPCRs, and other groups of receptors, are already available, currently, there is no publicly available database focusing on G Proteins and containing information about their coupling specificity with their respective receptors. DESCRIPTION: gpDB is a publicly accessible G proteins/GPCRs relational database. Including species homologs, the database contains detailed information for 418 G protein monomers (272 Gα, 87 Gβ and 59 Gγ) and 2782 GPCRs sequences belonging to families with known coupling to G proteins. The GPCRs and the G proteins are classified according to a hierarchy of different classes, families and sub-families, based on extensive literature searchs. The main innovation besides the classification of both G proteins and GPCRs is the relational model of the database, describing the known coupling specificity of the GPCRs to their respective α subunit of G proteins, a unique feature not available in any other database. There is full sequence information with cross-references to publicly available databases, references to the literature concerning the coupling specificity and the dimerization of GPCRs and the user may submit advanced queries for text search. Furthermore, we provide a pattern search tool, an interface for running BLAST against the database and interconnectivity with PRED-TMR, PRED-GPCR and TMRPres2D. CONCLUSIONS: The database will be very useful, for both experimentalists and bioinformaticians, for the study of G protein/GPCR interactions and for future development of predictive algorithms. It is available for academics, via a web browser at the URL:
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spelling pubmed-5443462005-01-14 A database for G proteins and their interaction with GPCRs Elefsinioti, Antigoni L Bagos, Pantelis G Spyropoulos, Ioannis C Hamodrakas, Stavros J BMC Bioinformatics Database BACKGROUND: G protein-coupled receptors (GPCRs) transduce signals from extracellular space into the cell, through their interaction with G proteins, which act as switches forming hetero-trimers composed of different subunits (α,β,γ). The α subunit of the G protein is responsible for the recognition of a given GPCR. Whereas specialised resources for GPCRs, and other groups of receptors, are already available, currently, there is no publicly available database focusing on G Proteins and containing information about their coupling specificity with their respective receptors. DESCRIPTION: gpDB is a publicly accessible G proteins/GPCRs relational database. Including species homologs, the database contains detailed information for 418 G protein monomers (272 Gα, 87 Gβ and 59 Gγ) and 2782 GPCRs sequences belonging to families with known coupling to G proteins. The GPCRs and the G proteins are classified according to a hierarchy of different classes, families and sub-families, based on extensive literature searchs. The main innovation besides the classification of both G proteins and GPCRs is the relational model of the database, describing the known coupling specificity of the GPCRs to their respective α subunit of G proteins, a unique feature not available in any other database. There is full sequence information with cross-references to publicly available databases, references to the literature concerning the coupling specificity and the dimerization of GPCRs and the user may submit advanced queries for text search. Furthermore, we provide a pattern search tool, an interface for running BLAST against the database and interconnectivity with PRED-TMR, PRED-GPCR and TMRPres2D. CONCLUSIONS: The database will be very useful, for both experimentalists and bioinformaticians, for the study of G protein/GPCR interactions and for future development of predictive algorithms. It is available for academics, via a web browser at the URL: BioMed Central 2004-12-24 /pmc/articles/PMC544346/ /pubmed/15619328 http://dx.doi.org/10.1186/1471-2105-5-208 Text en Copyright © 2004 Elefsinioti et al; licensee BioMed Central Ltd.
spellingShingle Database
Elefsinioti, Antigoni L
Bagos, Pantelis G
Spyropoulos, Ioannis C
Hamodrakas, Stavros J
A database for G proteins and their interaction with GPCRs
title A database for G proteins and their interaction with GPCRs
title_full A database for G proteins and their interaction with GPCRs
title_fullStr A database for G proteins and their interaction with GPCRs
title_full_unstemmed A database for G proteins and their interaction with GPCRs
title_short A database for G proteins and their interaction with GPCRs
title_sort database for g proteins and their interaction with gpcrs
topic Database
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC544346/
https://www.ncbi.nlm.nih.gov/pubmed/15619328
http://dx.doi.org/10.1186/1471-2105-5-208
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