1rtg

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spinqualitylabelsall models 1rtg, resolution 2.6Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

C-TERMINAL DOMAIN (HAEMOPEXIN-LIKE DOMAIN) OF HUMAN MATRIX METALLOPROTEINASE-2

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

In common with most other matrix metalloproteinases, gelatinase A has a, non-catalytic C-terminal domain that displays sequence homology to, haemopexin. Crystals of this domain were used by molecular replacement to, solve its molecular structure at 2.6 A resolution, which was refined to an, R value of 17.9%. This structure has a disc-like shape, with the chain, folded into a beta-propeller structure that has pseudo four-fold symmetry., Although the topology and the side-chain arrangement are very similar to, the equivalent domain of fibroblast collagenase, significant differences, in surface charge and contouring are observable on 1 side of the, gelatinase A disc. This difference might be a factor in allowing the, gelatinase A C-terminal domain to bind to natural inhibitor TIMP-2.

Disease

Known diseases associated with this structure: Osteolysis, idiopathic, Saudi type OMIM:[120360], Winchester syndrome OMIM:[120360]

About this Structure

1RTG is a Single protein structure of sequence from Homo sapiens with CL and CA as ligands. Active as Gelatinase A, with EC number 3.4.24.24 Full crystallographic information is available from OCA.

Reference

The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function., Gohlke U, Gomis-Ruth FX, Crabbe T, Murphy G, Docherty AJ, Bode W, FEBS Lett. 1996 Jan 8;378(2):126-30. PMID:8549817

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