Linked Life Data

8259210

Source:http://linkedlifedata.com/resource/pubmed/id/8259210

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6456
pubmed:dateCreated
1994-1-14
pubmed:abstractText
The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0028-0836
pubmed:author
pubmed:issnType
Print
pubmed:day
16
pubmed:volume
366
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
654-63
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8259210-Amino Acid Sequence, pubmed-meshheading:8259210-Animals, pubmed-meshheading:8259210-Catalysis, pubmed-meshheading:8259210-Cattle, pubmed-meshheading:8259210-Computer Graphics, pubmed-meshheading:8259210-Crystallography, X-Ray, pubmed-meshheading:8259210-Guanosine 5'-O-(3-Thiotriphosphate), pubmed-meshheading:8259210-Guanosine Diphosphate, pubmed-meshheading:8259210-Guanosine Triphosphate, pubmed-meshheading:8259210-Hydrolysis, pubmed-meshheading:8259210-Models, Molecular, pubmed-meshheading:8259210-Molecular Sequence Data, pubmed-meshheading:8259210-Phosphoric Diester Hydrolases, pubmed-meshheading:8259210-Protein Binding, pubmed-meshheading:8259210-Protein Conformation, pubmed-meshheading:8259210-Retinal Rod Photoreceptor Cells, pubmed-meshheading:8259210-Rhodopsin, pubmed-meshheading:8259210-Transducin
pubmed:year
1993
pubmed:articleTitle
The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.
pubmed:affiliation
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't