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PMID: 8552184 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The 2.0 A crystal structure of a heterotrimeric G protein.

Nature ·Vol. 379 ·No. 6563 ·1996-01-25 ·Pages 311-9

Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, Sigler PB

Abstract

The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the alpha and beta gamma subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the alpha but not of the beta gamma subunits. The location of the known sites for post-translational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor.

MeSH Terms
Amino Acid Sequence Animals Cattle Crystallography, X-Ray Escherichia coli GTP-Binding Proteins/chemistry,metabolism Guanosine Triphosphate/metabolism Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Processing, Post-Translational Receptors, Cell Surface/chemistry,metabolism Recombinant Proteins/chemistry Sequence Homology, Amino Acid
Chemicals
Receptors, Cell Surface Recombinant Proteins Guanosine Triphosphate GTP-Binding Proteins
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Lambright D G
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06510, USA.
Sondek J
Bohm A
Skiba N P
Hamm H E
Sigler P B
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1996-01-25
Pages
311-9
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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