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
Naturejournal_title
Natureauthors
Noel JP,Hamm HE,Sigler PBdoi
10.1038/366654a0subject
Has Abstractpub_date
1993-12-16 00:00:00pages
654-63issue
6456eissn
0028-0836issn
1476-4687journal_volume
366pub_type
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