MMP1
Description
The MMP1 (matrix metallopeptidase 1) is a protein-coding gene located on chromosome 11.
MMP1 (matrix metalloproteinase-1), also known as interstitial collagenase and fibroblast collagenase, is an enzyme produced by humans. The gene for MMP1, MMP1, is located on chromosome 11q22.3 and is part of a cluster of MMP genes. MMP1 was the first vertebrate collagenase to be both purified and cloned. It has an estimated molecular weight of 54 kDa. MMP1's structure includes a pre-domain, a pro-domain, a catalytic domain, a linker region, and a hemopexin-like domain. The catalytic domain of MMP1 is composed of five beta-strands, three alpha-helices, and eight loops. It contains five metal ions, three calcium ions (Ca2+), and two zinc ions (Zn2+), one of which plays a catalytic role. The catalytic domain starts with amino acid F100. The first x-ray structure of the catalytic domain was of a truncated form lacking the first seven amino acids.
MMP1 cleaves collagen types I, II, and III at a specific site within their helical domain. It also cleaves collagen types VII and X. In the context of HIV infection, MMP1 interacts with and cleaves the secreted viral Tat protein, which reduces Tat-mediated neurotoxicity.
MMP1 is also known as CLG, CLGN.
Associated Diseases
- Epidermolysis bullosa dystrophica, autosomal recessive
- Autosomal recessive generalized dystrophic epidermolysis bullosa, severe form
