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Mmp7

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Mmp7

Matrix metallopeptidase 7 (matrilysin, uterine)
PDB rendering based on 1mmp.
Available structures
PDB Ortholog search: RCSB
Identifiers
3.4.24.23
RNA expression pattern

Matrilysin also known as matrix metalloproteinase-7 (MMP-7) is an enzyme that in humans is encoded by the MMP7 gene.[1]

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]

References

Further reading

External links

  • The M10.008


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