4 GO Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR021158 |
| GO:0008270 | IPR021158 |
| GO:0006508 | IPR021158 |
| GO:0031012 | IPR021158 |
4 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR021158 |
| GO:0008270 | IPR021158 |
| GO:0006508 | IPR021158 |
| GO:0031012 | IPR021158 |
| Type: | Binding_site | Name: | Peptidase M10A, cysteine switch, zinc binding site |
| Description: | Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site []. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [].This group of metallopeptidases belong to the MEROPS peptidase family M10 (clan MA(M)), subfamily M10A. The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA.Sequences having this domain are extracellular metalloproteases, such as collagenase and stromelysin, which degrade the extracellular matrix, are known as matrixins. They are zinc-dependent,calcium-activated proteases synthesised as inactive precursors (zymogens), which are proteolytically cleaved to yield the active enzyme[, ]. All matrixins and related proteins possess 2 domains: an N-terminaldomain, and a zinc-binding active site domain. The N-terminal domain peptide, cleaved during the activation step, includes a conserved PRCGVPDVoctapeptide, known as the cysteine switch, whose Cys residue chelates the active site zinc atom, rendering the enzyme inactive [, ]. The active enzymedegrades components of the extracellular matrix, playing a role in the initial steps of tissue remodelling during morphogenesis, wound healing,angiogenesis and tumour invasion [, ]. | Short Name: | Pept_M10A_Zn_BS |
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR021158 |
| GO:0008270 | IPR021158 |
| GO:0006508 | IPR021158 |
| GO:0031012 | IPR021158 |
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR021158 |
| GO:0008270 | IPR021158 |
| GO:0006508 | IPR021158 |
| GO:0031012 | IPR021158 |
