This HTML5 document contains 18 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

PrefixNamespace IRI
dctermshttp://purl.org/dc/terms/
vivohttp://vivoweb.org/ontology/core#
marcrelhttp://id.loc.gov/vocabulary/relators/
n8http://orcid.org/0000-0002-7620-6895#
bibohttp://purl.org/ontology/bibo/
n9http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_13/
n17http://hub.abes.fr/acs/periodical/jacsat/
rdachttp://rdaregistry.info/Elements/c/
n14http://hub.abes.fr/acs/periodical/articletype/
hubhttp://hub.abes.fr/namespace/
rdfhttp://www.w3.org/1999/02/22-rdf-syntax-ns#
n16http://orcid.org/0000-0003-4666-8834#
n7http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_13/101021ja077268b/m/
rdawhttp://rdaregistry.info/Elements/w/
n2http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_13/101021ja077268b/
n5http://hub.abes.fr/referentiel/acs/documenttypename/subject/
xsdhhttp://www.w3.org/2001/XMLSchema#
n11http://hub.abes.fr/acs/periodical/jacsat/2008/volume_130/issue_13/101021ja077268b/authorship/
Subject Item
n2:w
rdf:type
bibo:Article rdac:C10001
dcterms:isPartOf
n9:w
dcterms:subject
n5:article
dcterms:title
Mechanisms of Inter- and Intramolecular Communication inGPCRs and G Proteins
rdaw:P10072
n7:print n7:web
vivo:relatedBy
n11:3 n11:4 n11:1 n11:2
marcrel:aut
n2:debenedettipierg n8:person n2:raimondifrancesco n16:person
dcterms:abstract
This study represents the first attempt to couple, by computational experiments, the mechanismsof intramolecular and intermolecular communication concerning a guanidine nucleotide exchange factor(GEF), the thromboxane A2 receptor (TXA2R), and the cognate G protein (Gq) in its heterotrimeric GDP-bound state. Two-way pathways mediate the communication between the receptor−G protein interfaceand both the agonist binding site of the receptor and the nucleotide binding site of the G protein. Theincrease in solvent accessibility in the neighborhoods of the highly conserved E/DRY receptor motif, inresponse to agonist binding, is instrumental in favoring the penetration of the C-terminus of Gqα in betweenthe cytosolic ends of H3, H5, and H6. The arginine of the E/DRY motif is predicted to be an importantmediator of the intramolecular and intermolecular communication involving the TXA2R. The receptor−Gprotein interface is predicted to involve multiple regions from the receptor and the G protein α-subunit.However, receptor contacts with the C-terminus of the α5-helix seem to be the major players in the receptor-catalyzed motion of the α-helical domain with respect to the Ras-like domain and in the formation of anucleotide exit route in between the αF-helix and β6/α5 loop of Gqα. The inferences from this study are ofwide interest, as they are expected to apply to the whole rhodopsin family, given also the considerable Gprotein promiscuity.
hub:articleType
n14:researcharticle
hub:isPartOfThisJournal
n17:w