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PMID: 9434906 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

G proteins, effectors and GAPs: structure and mechanism.

Current opinion in structural biology ·Vol. 7 ·No. 6 ·1997-12-00 ·Pages 849-56

Sprang SR

Abstract

G proteins from a diverse family of regulatory GTPases which, in the GTP-bound state, bind to and activate downstream effectors. Structures of Ras homologs bound to effector domains have revealed mechanisms by which G proteins couple GTP binding to effector activation and achieve specificity. Complexes between structurally unrelated GTPase-activating proteins with complementary G proteins suggest common mechanisms by which GTP hydrolysis is stimulated via direct interactions with conformationally labile switch regions of the G protein.

MeSH Terms
Binding Sites GTP Phosphohydrolases/chemistry,metabolism GTP-Binding Proteins/chemistry,metabolism GTPase-Activating Proteins Guanosine Triphosphate/chemistry,metabolism Models, Molecular Protein Binding Protein Conformation Proteins/chemistry,metabolism Proto-Oncogene Proteins p21(ras)/chemistry,metabolism ras GTPase-Activating Proteins ras Proteins/chemistry,metabolism
Chemicals
GTPase-Activating Proteins Proteins ras GTPase-Activating Proteins Guanosine Triphosphate GTP Phosphohydrolases GTP-Binding Proteins Proto-Oncogene Proteins p21(ras) ras Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Sprang S R
Howard Hughes Medical Institute, University of Texas, Southwestern Medical Center, Dallas 75235-9050, USA. sprang@howie.swmed.edu
Article Info
Journal
Current opinion in structural biology
Abbr.
Curr Opin Struct Biol
ISSN
0959-440X
Published
1997-12-00
Pages
849-56
Language
English
Region
England
NLM ID
9107784
Subset
IM
Grants
NIDDK NIH HHS · DK46371 · United States
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