The 2.2 A crystal structure of transducin-alpha complexed with GTP gamma S.

Abstract:

:The 2.2 A crystal structure of activated rod transducin, Gt alpha.GTP gamma S, shows the bound GTP gamma S molecule occluded deep in a cleft between a domain structurally homologous to small GTPases and a helical domain unique to heterotrimeric G proteins. The structure, when combined with biochemical and genetic studies, suggests: how an activated receptor might open this cleft to allow nucleotide exchange; a mechanism for GTP-induced changes in effector and receptor binding surfaces; and a mechanism for GTPase activity not evident from previous data.

journal_name

Nature

journal_title

Nature

authors

Noel JP,Hamm HE,Sigler PB

doi

10.1038/366654a0

subject

Has Abstract

pub_date

1993-12-16 00:00:00

pages

654-63

issue

6456

eissn

0028-0836

issn

1476-4687

journal_volume

366

pub_type

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