| Literature DB >> 8552184 |
D G Lambright1, J Sondek, A Bohm, N P Skiba, H E Hamm, P B Sigler.
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：
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Year: 1996 PMID： 8552184 DOI： 10.1038/379311a0
Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962