1ck7

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(New page: 200px<br /> <applet load="1ck7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ck7, resolution 2.8&Aring;" /> '''GELATINASE A (FULL-L...)
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Revision as of 14:16, 12 November 2007

Image:1ck7.gif

1ck7, resolution 2.8Å

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GELATINASE A (FULL-LENGTH)

Contents

Overview

Matrix metalloproteinases (MMPs) catalyze extracellular matrix, degradation. Control of their activity is a promising target for therapy, of diseases characterized by abnormal connective tissue turnover. MMPs are, expressed as latent proenzymes that are activated by proteolytic cleavage, that triggers a conformational change in the propeptide (cysteine switch)., The structure of proMMP-2 reveals how the propeptide shields the catalytic, cleft and that the cysteine switch may operate through cleavage of loops, essential for propeptide stability.

Disease

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

About this Structure

1CK7 is a Single protein structure of sequence from Homo sapiens with ZN, CA, CL, NA and SO4 as ligands. Active as Gelatinase A, with EC number 3.4.24.24 Full crystallographic information is available from OCA.

Reference

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed., Morgunova E, Tuuttila A, Bergmann U, Isupov M, Lindqvist Y, Schneider G, Tryggvason K, Science. 1999 Jun 4;284(5420):1667-70. PMID:10356396

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