2d1o

From Proteopedia

---

Revision as of 19:19, 12 November 2007

proteopedia linkproteopedia link

spinqualitylabelsall models 2d1o, resolution 2.02Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Stromelysin-1 (MMP-3) complexed to a hydroxamic acid inhibitor

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3), and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453 have, been solved at 2.01 and 2.37A resolutions, respectively. The results, revealed that the binding modes for this inhibitor to MMP-3 and -13 were, quite similar. However, subtle comparative differences were observed at, the bottom of S1' pockets, which were occupied with the guanidinomethyl, moiety of the inhibitor. A remarkable feature of the inhibitor was the, deep penetration of its long aliphatic chain into the S1' pocket and, exposure of the guanidinomethyl moiety to the solvent.

Disease

Known diseases associated with this structure: Coronary heart disease, susceptibility to OMIM:[185250]

About this Structure

2D1O is a Single protein structure of sequence from Homo sapiens with ZN, CA and FA4 as ligands. Active as Stromelysin 1, with EC number 3.4.24.17 Full crystallographic information is available from OCA.

Reference

Crystal structures of the catalytic domain of human stromelysin-1 (MMP-3) and collagenase-3 (MMP-13) with a hydroxamic acid inhibitor SM-25453., Kohno T, Hochigai H, Yamashita E, Tsukihara T, Kanaoka M, Biochem Biophys Res Commun. 2006 May 26;344(1):315-22. Epub 2006 Mar 27. PMID:16603129

Page seeded by OCA on Mon Nov 12 21:25:30 2007