1gdd

Publication Abstract from PubMed

Crystallographic analysis of 2.2 angstrom resolution shows that guanosine triphosphate (GTP) hydrolysis triggers conformational changes in the heterotrimeric G-protein alpha subunit, Gi alpha 1. The switch II and switch III segments become disordered, and linker II connecting the Ras and alpha helical domains moves, thus altering the structures of potential effector and beta gamma binding regions. Contacts between the alpha-helical and Ras domains are weakened, possibly facilitating the release of guanosine diphosphate (GDP). The amino and carboxyl termini, which contain receptor and beta gamma binding determinants, are disordered in the complex with GTP, but are organized into a compact microdomain on GDP hydrolysis. The amino terminus also forms extensive quaternary contacts with neighboring alpha subunits in the lattice, suggesting that multimers of alpha subunits or heterotrimers may play a role in signal transduction.

Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis.,Mixon MB, Lee E, Coleman DE, Berghuis AM, Gilman AG, Sprang SR Science. 1995 Nov 10;270(5238):954-60. PMID:7481799^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.