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

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.

SUBMITTER: Opatowsky Y 

PROVIDER: S-EPMC1934412 | biostudies-literature | 2006 Oct

REPOSITORIES: biostudies-literature