Linked Life Data

9753695

Source:http://linkedlifedata.com/resource/pubmed/id/9753695

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1998-12-3
pubmed:databankReference
pubmed:abstractText
Inactive heterotrimeric G proteins are composed of a GDP-bound alpha subunit (Galpha) and a stable heterodimer of Gbeta and Ggamma subunits. Upon stimulation by a receptor, Galpha subunits exchange GDP for GTP and dissociate from Gbetagamma, both Galpha and Gbetagamma then interact with downstream effectors. Isoforms of Galpha, Gbeta and Ggamma potentially give rise to many heterotrimeric combinations, limited in part by amino acid sequence differences that lead to selective interactions. The mechanism by which GTP promotes Gbetagamma dissociation is incompletely understood. The Gly203-->Ala mutant of Gialpha1 binds and hydrolyzes GTP normally but does not dissociate from Gbetagamma, demonstrating that GTP binding and activation can be uncoupled. Structural data are therefore important for understanding activation and subunit recognition in G protein heterotrimers.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0969-2126
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1169-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Structural basis of activity and subunit recognition in G protein heterotrimers.
pubmed:affiliation
Department of Biochemistry The University of Texas Southwestern Medical Center 5323 Harry Hines Boulevard, Dallas, TX 75235-9050, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't