MMP7
From Wikipedia, the free encyclopedia
Matrilysin also known as matrix metalloproteinase-7 (MMP-7) is an enzyme that in humans is encoded by the MMP7 gene.[1]
[edit] Function
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades proteoglycans, fibronectin, elastin and casein and differs from most MMP family members in that it lacks a conserved C-terminal protein domain. The enzyme is involved in wound healing, and studies in mice suggest that it regulates the activity of defensins in intestinal mucosa. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[2]
[edit] References
[edit] Further reading
[edit] External links
- The MEROPS online database for peptidases and their inhibitors: M10.008
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PDB gallery
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1mmp: MATRILYSIN COMPLEXED WITH CARBOXYLATE INHIBITOR
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1mmq: MATRILYSIN COMPLEXED WITH HYDROXAMATE INHIBITOR
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1mmr: MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR
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2ddy: Solution Structure of Matrilysin (MMP-7) Complexed to Constraint Conformational Sulfonamide Inhibitor
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