dc.contributorUniversidade Federal de São Paulo (UNIFESP)
dc.contributorEMBL
dc.creatorOliveira, Laerte [UNIFESP]
dc.creatorPaiva, Antonio Cechelli de Mattos [UNIFESP]
dc.creatorVriend, Gerrit
dc.date.accessioned2016-01-24T11:40:15Z
dc.date.accessioned2023-09-04T19:21:34Z
dc.date.available2016-01-24T11:40:15Z
dc.date.available2023-09-04T19:21:34Z
dc.date.created2016-01-24T11:40:15Z
dc.date.issued1993-12-01
dc.identifierJournal of Computer-aided Molecular Design. Leiden: Escom Sci Publ Bv, v. 7, n. 6, p. 649-658, 1993.
dc.identifier0920-654X
dc.identifierhttp://repositorio.unifesp.br/handle/11600/25367
dc.identifier10.1007/BF00125323
dc.identifierWOS:A1993MU48100002
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8625576
dc.description.abstractG-protein-coupled receptors all share the seven transmembrane helix motif similar to bacteriorhodopsin. This similarity was exploited to build models for these receptors. From an analysis of a multi-sequence alignment of 225 G-protein-coupled receptors belonging to the rhodopsin-like superfamily, conclusions could be drawn about functional residues. Seven residues in the transmembrane regions are conserved throughout all aligned receptors. These residues cluster at the cytosolic side of the transmembrane helices and are for all rhodopsin-like G-protein-coupled receptors implied in signal transduction. An analysis of correlated mutations reveals a number of residues, both in the helices and in the cytosolic loops, that might be important in the signal transduction pathway in subfamilies of this receptor family.
dc.languageeng
dc.publisherEscom Sci Publ Bv
dc.relationJournal of Computer-aided Molecular Design
dc.rightsAcesso restrito
dc.subjectG-PROTEIN-COUPLED RECEPTORS
dc.subjectMODELING
dc.titleA common motif in G-protein-coupled seven transmembrane helix receptors
dc.typeArtigo


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