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FEBS Lett. 2006 Oct 30;580(25):5959-64. Epub 2006 Oct 6.

Structure-function studies of the G-domain from human gem, a novel small G-protein.

Author information

1
Department of Biochemistry, Daniella Rich Institute for Structural Biology, Tel Aviv University, Ramat Aviv 69978, Israel.

Abstract

Gem, a member of the Rad,Gem/Kir subfamily of small G-proteins, has unique sequence features. We report here the crystallographic structure determination of the Gem G-domain in complex with nucleotide to 2.4 A resolution. Although the basic Ras protein fold is maintained, the Gem switch regions emphatically differ from the Ras paradigm. Our ensuing biochemical characterization indicates that Gem G-domain markedly prefers GDP over GTP. Two known functions of Gem are distinctly affected by spatially separated clusters of mutations.

PMID:
17052716
PMCID:
PMC1934412
DOI:
10.1016/j.febslet.2006.09.067
[Indexed for MEDLINE]
Free PMC Article

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