The 2.0 Å crystal structure of a heterotrimeric G protein

• Published in: Nature (London) Vol. 379; no. 6563; pp. 311 - 319
• Main Authors: Lambright, David G, Sondek, John, Bohm, Andrew, Skiba, Nikolai P, Hamm, Heidi E, Sigler, Paul B
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 25-01-1996
• Subjects: Amino Acid Sequence; Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Biological and medical sciences; Cattle; Crystallography, X-Ray; Escherichia coli; Fundamental and applied biological sciences. Psychology; GTP-Binding Proteins - chemistry; GTP-Binding Proteins - metabolism; Guanosine Triphosphate - metabolism; Humans; Models, Molecular; Molecular Sequence Data; Protein Conformation; Protein Processing, Post-Translational; Proteins; Receptors, Cell Surface - chemistry; Receptors, Cell Surface - metabolism; Recombinant Proteins - chemistry; Sequence Homology, Amino Acid; Binding protein; Signal transduction; GTP; Regulation(control); Molecular interaction; Subunit; Structural analysis; G protein; Biological receptor; Crystalline structure
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/379311a0

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.