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The 2.0 Å crystal structure of a heterotrimeric G protein

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.

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Lambright, D., Sondek, J., Bohm, A. et al. The 2.0 Å crystal structure of a heterotrimeric G protein. Nature 379, 311–319 (1996). https://doi.org/10.1038/379311a0

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