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. 1996 Jan 25;379(6563):311-9.
doi: 10.1038/379311a0.

The 2.0 A crystal structure of a heterotrimeric G protein

D G Lambright  1 , J Sondek, A Bohm, N P Skiba, H E Hamm, P B Sigler
Affiliations

The 2.0 A crystal structure of a heterotrimeric G protein

D G Lambright et al. Nature. .

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.

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Comment in

  • The G-protein nanomachine.
    Clapham DE. Clapham DE. Nature. 1996 Jan 25;379(6563):297-9. doi: 10.1038/379297a0. Nature. 1996. PMID: 8552180 No abstract available.

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