2cm3

From Proteopedia

Revision as of 15:07, 30 October 2007

STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B (C2)

Overview

Crystal structures of protein-tyrosine phosphatase 1B in complex with, compounds bearing a novel isothiazolidinone (IZD) heterocyclic phosphonate, mimetic reveal that the heterocycle is highly complementary to the, catalytic pocket of the protein. The heterocycle participates in an, extensive network of hydrogen bonds with the backbone of the, phosphate-binding loop, Phe(182) of the flap, and the side chain of, Arg(221). When substituted with a phenol, the small inhibitor induces the, closed conformation of the protein and displaces all waters in the, catalytic pocket. Saturated IZD-containing peptides are more potent, inhibitors than unsaturated analogs because the IZD heterocycle and phenyl, ring directly attached to it bind in a nearly orthogonal orientation with, respect to each ... [(full description)]

About this Structure

2CM3 is a [Single protein] structure of sequence from [Homo sapiens] with CA as [ligand]. Active as [Protein-tyrosine-phosphatase], with EC number [3.1.3.48]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Structural basis for inhibition of protein-tyrosine phosphatase 1B by isothiazolidinone heterocyclic phosphonate mimetics., Ala PJ, Gonneville L, Hillman MC, Becker-Pasha M, Wei M, Reid BG, Klabe R, Yue EW, Wayland B, Douty B, Polam P, Wasserman Z, Bower M, Combs AP, Burn TC, Hollis GF, Wynn R, J Biol Chem. 2006 Oct 27;281(43):32784-95. Epub 2006 Aug 17. PMID:16916797

Page seeded by OCA on Tue Oct 30 17:12:16 2007