The 2.0 Å crystal structure of a heterotrimeric G protein View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1996-01

AUTHORS

David G. Lambright, John Sondek, Andrew Bohm, Nikolai P. Skiba, Heidi E. Hamm, Paul B. Sigler

ABSTRACT

The structure of a heterotrimeric G protein reveals the mechanism of the nucleotide-dependent engagement of the α and βγ subunits that regulates their interaction with receptor and effector molecules. The interaction involves two distinct interfaces and dramatically alters the conformation of the αbut not of theβγ subunits. The location of the known sites for posttranslational modification and receptor coupling suggest a plausible orientation with respect to the membrane surface and an activated heptahelical receptor. More... »

PAGES

311-319

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/379311a0

DOI

http://dx.doi.org/10.1038/379311a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048752425

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8552184


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