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The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.

Abstract:

The hydrolysis of collagen (collagenolysis) is one of the committed steps in extracellular matrix turnover. Within the matrix metalloproteinase (MMP) family distinct preferences for collagen types are seen. The substrate determinants that may guide these specificities are unknown. In this study, we have utilized 12 triple-helical substrates in combination with 10 MMPs to better define the contributions of substrate sequence and thermal stability toward triple helicase activity and collagen sp...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m606004200

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Journal:
Journal of biological chemistry
Volume:
281
Issue:
50
Pages:
38302-38313
Publication date:
2006-12-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Source identifiers:
227294

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