The 2.0 A crystal structure of a heterotrimeric G protein.

Lambright DG, Sondek J, Bohm A, Skiba NP, Hamm HE, Sigler PB
Nature. 1996 379 (6563): 311-9

PMID: 8552184 · 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.

MeSH Terms (15)

Amino Acid Sequence Animals Cattle Crystallography, X-Ray Escherichia coli GTP-Binding Proteins Guanosine Triphosphate Humans Models, Molecular Molecular Sequence Data Protein Conformation Protein Processing, Post-Translational Receptors, Cell Surface Recombinant Proteins Sequence Homology, Amino Acid

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