This gene encodes a member of the matrix metalloproteinase (MMP) family of proteins. These proteins are involved in the breakdown of extracellular matrix in embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Proteolysis at different sites on this protein results in multiple active forms of the enzyme with distinct N-termini. MMP-8 also called neutrophil collagenase or collagenase 2, collagenases are characterized for their abilities to cleave triple-helical regions of interstitial collagnes (types I, II, and III) at a site about three-fourths away from the N-terminus. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. Alternative splicing results in multiple transcript variants.[1]
To see
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Structure
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Thanks to X-ray crystallography, the structure of 2OY4 has been solved with 1,7 Å resolution. This enzyme consists of and .
Pocket interaction
Ca2+
Zn2+
Function
The MMPs are secreted as inactive proproteins and then activated after a cleavage by extracellular proteinases.
Disease
Relevance
Structural highlights
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