Protein farnesyltransferase.
In the past year, the crystal structure of alpha beta heterodimeric protein farnesyltransferase from rat was reported to a resolution of 2.25 A. Farnesyltransferase catalyzes the essential post-translational lipidation of Ras and several other cellular signal transduction proteins. The structure provides a foundation for understanding the specificity and mechanism of protein prenylation and may aid in the design of new anticancer therapeutics.
Park
H W
HW
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Beese
L S
LS
D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D019281:Dimerization; D008958:Models, Molecular; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017368:Protein Prenylation; D017433:Protein Structure, Secondary; D051381:Rats; D013379:Substrate Specificity; D015032:Zinc / Q000378:metabolism; D018631:ras Proteins / Q000378:metabolism
D019883:Alkyl and Aryl Transferases; C064911:p21(ras) farnesyl-protein transferase; D018631:ras Proteins; D015032:Zinc