title: Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
authors.affiliation: Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
authors.forename: T Scott
authors.initials: TS
authors.lastname: Reid
authors.forename: Kimberly L
authors.initials: KL
authors.lastname: Terry
authors.forename: Patrick J
authors.initials: PJ
authors.lastname: Casey
authors.forename: Lorena S
authors.initials: LS
authors.lastname: Beese
mesh_terms: D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray; D015195:Drug Design; D006801:Humans; D008954:Models, Biological; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017368:Protein Prenylation; D013379:Substrate Specificity
chemical_list: D010455:Peptides; D019883:Alkyl and Aryl Transferases; C083291:geranylgeranyltransferase type-I; C064911:p21(ras) farnesyl-protein transferase