| Literature DB >> 8208289 |
D G Lambright1, J P Noel, H E Hamm, P B Sigler.
Abstract
The 1.8 A crystal structure of transducin alpha.GDP, when compared to that of the activated complex with GTP-gamma S, reveals the nature of the conformational changes that occur on activation of a heterotrimeric G-protein alpha-subunit. Structural changes initiated by direct contacts with the terminal phosphate of GTP propagate to regions that have been implicated in effector activation. The changes are distinct from those observed in other members of the GTPase superfamily.Entities:
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Year: 1994 PMID: 8208289 DOI: 10.1038/369621a0
Source DB: PubMed Journal: Nature ISSN: 0028-0836 Impact factor: 49.962