Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6184
pubmed:dateCreated
1988-9-26
pubmed:abstractText
Membrane-bound G proteins carry information from receptors on the outside of cells to effector proteins inside cells. The alpha subunits of these heterotrimeric proteins bind and hydrolyse GTP and control the specificity of interactions with receptor and effector elements. Signalling by G proteins involves a cycle in which the inactive alpha beta gamma-GDP complex dissociates to produce alpha*-GTP, which is capable of activating the effector enzyme or ion channel; the alpha*-GTP complex hydrolyses bound GTP and reassociates with beta gamma to form the inactive complex. We have characterized a mutation that interrupts this GTP-driven cycle in alpha s, the alpha-chain of Gs, the G protein that stimulates adenylyl cyclase. The mutation converts a glycine to an alanine residue in the presumed GDP-binding domain of alpha s. The location and biochemical consequences of this mutation suggest a common mechanism by which binding of GTP or ATP may induce changes in the conformation of a number of nucleoside triphosphate binding proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/Aluminum, http://linkedlifedata.com/resource/pubmed/chemical/Aluminum Compounds, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/Fluorides, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Guanylyl Imidodiphosphate, http://linkedlifedata.com/resource/pubmed/chemical/Magnesium, http://linkedlifedata.com/resource/pubmed/chemical/Trypsin, http://linkedlifedata.com/resource/pubmed/chemical/aluminum fluoride
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
334
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
712-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed-meshheading:3137475-Adenosine Triphosphate, pubmed-meshheading:3137475-Adenylate Cyclase, pubmed-meshheading:3137475-Aluminum, pubmed-meshheading:3137475-Aluminum Compounds, pubmed-meshheading:3137475-Animals, pubmed-meshheading:3137475-Binding Sites, pubmed-meshheading:3137475-Cell Membrane, pubmed-meshheading:3137475-DNA, pubmed-meshheading:3137475-Fluorides, pubmed-meshheading:3137475-GTP-Binding Proteins, pubmed-meshheading:3137475-Guanosine Diphosphate, pubmed-meshheading:3137475-Guanosine Triphosphate, pubmed-meshheading:3137475-Guanylyl Imidodiphosphate, pubmed-meshheading:3137475-Lymphoma, pubmed-meshheading:3137475-Magnesium, pubmed-meshheading:3137475-Mice, pubmed-meshheading:3137475-Mutation, pubmed-meshheading:3137475-Protein Conformation, pubmed-meshheading:3137475-Trypsin, pubmed-meshheading:3137475-Tumor Cells, Cultured
pubmed:year
1988
pubmed:articleTitle
A mutation that prevents GTP-dependent activation of the alpha chain of Gs.
pubmed:affiliation
Department of Pharmacology, University of California, San Francisco 94143-0450.
pubmed:publicationType
Journal Article