MMP1

There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases).

The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X (PubMed:1645757, PubMed:2153297, PubMed:2557822). In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity (PubMed:16807369).

Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.

Tyrosine phosphorylated in platelets by PKDCC/VLK.

Belongs to the peptidase M10A family.

• Secreted
• Extracellular space
• Extracellular matrix

CLG, MMP1, Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1

• entrezGene:4312
• omim:120353
• swissprot:P03956

Proteins

Immunology & Infectious Disease

54007Da