1rts

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1rts, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

THYMIDYLATE SYNTHASE FROM RAT IN TERNARY COMPLEX WITH DUMP AND TOMUDEX

Overview

Two crystal structures of rat thymidylate synthase (TS) complexed with, dUMP and the anticancer drug Tomudex (ZD1694) have been determined to, resolutions of 3.3 and 2.6 A. Tomudex is one of several new antifolates, targeted to TS and the first to be approved for clinical use. The, structures represent the first views of any mammalian TS bound to ligands, and suggest that the rat protein undergoes a ligand-induced conformational, change similar to that of the Escherichia coli protein. Surprisingly, Tomudex does not induce the "closed" conformation in rat TS that is seen, on binding to E. coli TS, resulting in inhibitor atoms that differ in, position by more than 1.5 A. Several species-specific differences in, sequence may be the reason for this. Phe 74 shifts to a new position in, the rat ... [(full description)]

About this Structure

1RTS is a [Single protein] structure of sequence from [Rattus norvegicus] with UMP and D16 as [ligands]. Active as [[1]], with EC number [2.1.1.45]. Full crystallographic information is available from [OCA].

Reference

Crystal structures of rat thymidylate synthase inhibited by Tomudex, a potent anticancer drug., Sotelo-Mundo RR, Ciesla J, Dzik JM, Rode W, Maley F, Maley GF, Hardy LW, Montfort WR, Biochemistry. 1999 Jan 19;38(3):1087-94. PMID:9894005

Page seeded by OCA on Mon Oct 29 20:48:47 2007