1su3

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spinqualitylabelsall models 1su3, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

X-ray structure of human proMMP-1: New insights into collagenase action

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Vertebrate collagenases, members of the matrix metalloproteinase (MMP), family, initiate interstitial fibrillar collagen breakdown. It is, essential in many biological processes, and unbalanced collagenolysis is, associated with diseases such as arthritis, cancer, atherosclerosis, aneurysm, and fibrosis. These metalloproteinases are secreted from the, cell as inactive precursors, procollagenases (proMMPs). To gain insights, into the structural basis of their activation mechanisms and collagen, binding, we have crystallized recombinant human proMMP-1 and determined, its structure to 2.2 A resolution. The catalytic metalloproteinase domain, and the C-terminal hemopexin (Hpx) domain show the classical MMP-fold, but, the structure has revealed new features in surface loops and domain, interaction. The prodomain is formed by a three-helix bundle and gives, insight into the stepwise activation mechanism of proMMP-1. The prodomain, interacts with the Hpx domain, which affects the position of the Hpx, domain relative to the catalytic domain. This interaction results in a, "closed" configuration of proMMP-1 in contrast to the "open" configuration, observed previously for the structure of active MMP-1. This is the first, evidence of mobility of the Hpx domain in relation to the catalytic, domain, providing an important clue toward the understanding of the, collagenase-collagen interaction and subsequent collagenolysis.

Disease

Known diseases associated with this structure: COPD, rate of decline of lung function in OMIM:[120353]

About this Structure

1SU3 is a Single protein structure of sequence from Homo sapiens with CA, CL, NA, ZN, SO4 and EPE as ligands. Active as Interstitial collagenase, with EC number 3.4.24.7 Full crystallographic information is available from OCA.

Reference

X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding., Jozic D, Bourenkov G, Lim NH, Visse R, Nagase H, Bode W, Maskos K, J Biol Chem. 2005 Mar 11;280(10):9578-85. Epub 2004 Dec 15. PMID:15611040

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