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1ck7
From Proteopedia
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[[Image:1ck7.gif|left|200px]] | [[Image:1ck7.gif|left|200px]] | ||
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'''GELATINASE A (FULL-LENGTH)''' | '''GELATINASE A (FULL-LENGTH)''' | ||
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[[Category: Tryggvason, K.]] | [[Category: Tryggvason, K.]] | ||
[[Category: Tuuttila, A.]] | [[Category: Tuuttila, A.]] | ||
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| - | [[Category: | + | [[Category: Metalloproteinase]] |
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Revision as of 09:49, 2 May 2008
GELATINASE A (FULL-LENGTH)
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.
About this Structure
1CK7 is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 12:49:27 2008
