Publication Abstract from PubMed
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.
Structure-function studies of the G-domain from human gem, a novel small G-protein.,Opatowsky Y, Sasson Y, Shaked I, Ward Y, Chomsky-Hecht O, Litvak Y, Selinger Z, Kelly K, Hirsch JA FEBS Lett. 2006 Oct 30;580(25):5959-64. Epub 2006 Oct 6. PMID:17052716[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
