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Papers In Press, published online ahead of print February 13, 2006
J. Lipid Res., doi:10.1194/jlr.R600002-JLR200
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Biochemistry Dept., Duke University Medical Center, Durham, NC 27710
Corresponding Author: lsb{at}biochem.duke.edu
More than a hundred proteins necessary for eukaryotic cell growth, differentiation, and morphology require post-translational modification by the covalent attachment of an isoprenoid lipid (prenylation). Prenylated proteins include members of the Ras, Rab and Rho families, lamins, CENPE and F, and the gamma subunit of many small heterotrimeric G proteins. This modification is catalyzed by the protein prenyltransferases: protein farnesyltransferase (FTase), protein geranylgeranyltransferase type I (GGTase-I), and protein geranylgeranyltransferase type II (GGTase-II, or RabGGTase). In this review, we examine the structural biology of FTase and GGTase-I (the CaaX prenyltransferases) to establish a framework for understanding the molecular basis of substrate specificity and mechanism. These enzymes have been identified in a number of species, including mammals, fungi, plants, and protists. Prenyltransferase structures include complexes that represent the major steps along the reaction path, as well as a number of complexes with clinically-relevant inhibitors. Such complexes may assist in the design of inhibitors that may lead to treatments of cancer, viral infection, and a number of deadly parasitic diseases.
Revised on February 9, 2006
Accepted on February 13, 2006
Structural biology of protein farnesyltransferase and geranylgeranyltransferase type-I
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