Sandbox Reserved 1125: Difference between revisions
From Proteopedia
Jump to navigationJump to search
Laura Dutto (talk | contribs) No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
== Matrix metalloproteinase-8 == | == Matrix metalloproteinase-8 == | ||
''MMP-8'', also called, ''Neutrophil collagenase'' or ''Collagenase 2'', is a zinc-dependent and calcium-dependent enzyme. It belongs to the [[Matrix metalloproteinase]]<br /> (MMP) family which is 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. The gene coding this family is localized on the chromosome 11 of Homo sapiens with 467 residues.<ref>[http://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4317 "MMP-8 matrix metallopeptidase 8 (neutrophil collagenase)"]</ref> | ''MMP-8'', also called, ''Neutrophil collagenase'' or ''Collagenase 2'', is a zinc-dependent and calcium-dependent enzyme. It belongs to the [[Matrix metalloproteinase]]<br /> (MMP) family which is 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. The gene coding this family is localized on the chromosome 11 of Homo sapiens with 467 residues.<ref>[http://www.ncbi.nlm.nih.gov/gene?Db=gene&Cmd=ShowDetailView&TermToSearch=4317 "MMP-8 matrix metallopeptidase 8 (neutrophil collagenase)"]</ref> | ||
To reload the initial structure of the catalytic domain of MMP-8, when looking at this page, click | |||
<scene name='71/719866/Mmp-8/3'>here</scene>. | |||
<StructureSection load='2oy4' size='340' side='right' caption='MMP-8 catalytic domain' scene='71/719866/Mmp-8/3'> | <StructureSection load='2oy4' size='340' side='right' caption='MMP-8 catalytic domain' scene='71/719866/Mmp-8/3'> | ||
| Line 73: | Line 76: | ||
The Cys1 residue is crucial for the inhibitor effect of TIMPs because it can interact with the catalytic zinc of the MMPs. The result is a chelation of the zinc by the N-terminal amino group and the carbonyl group of Cys1.<ref>PMID:16405877</ref> Moreover, this interaction triggers the expulsion of the water molecule which was bound to the zinc. | The Cys1 residue is crucial for the inhibitor effect of TIMPs because it can interact with the catalytic zinc of the MMPs. The result is a chelation of the zinc by the N-terminal amino group and the carbonyl group of Cys1.<ref>PMID:16405877</ref> Moreover, this interaction triggers the expulsion of the water molecule which was bound to the zinc. | ||
No structures of MMP-8 with TIMPs are available on PDB. However, the mecanism of inhibition is common to all the MMPs. | No structures of MMP-8 with TIMPs are available on PDB. However, the mecanism of inhibition is common to all the MMPs. To see the interaction between the catalytic domain of MMP-3 and TIMP-1 (in green) click <scene name='71/719866/Timp1/4'>here</scene>.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=1UEA "Metalloprotease-inhibitor Complex"]</ref> | ||
=== Synthetic inhibitors === | === Synthetic inhibitors === | ||
