Receptor-G protein coupling is established by a potential conformational switch in the βγ complex

O. Kisselev, A. Pronin, M. Ermolaeva, N. Gautam

Research output: Contribution to journalArticle

92 Scopus citations

Abstract

Receptor-G protein interaction is characterized by cycles of association and dissociation. We present evidence which indicates that during receptor-G protein interaction, the C-terminal tail of the G protein γ subunit, which is masked in the βγ complex, is exposed and establishes high-affinity contact with the receptor. This potential conformational switch provides a mechanism to regulate receptor-G protein coupling. This switch may also be significant for the role of the βγ complex in regulation of effector function.

Original languageEnglish
Pages (from-to)9102-9106
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number20
DOIs
StatePublished - Sep 26 1995

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