Collagenase (non-MMP): Difference between revisions
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**[[4are]] - ChColG residues 119-790<br /> | **[[4are]] - ChColG residues 119-790<br /> | ||
**[[2y6i]] - ChColG residues 119-880 + peptide<br /> | **[[2y6i]] - ChColG residues 119-880 + peptide<br /> | ||
**[[4jrw]], [[4tn9 | **[[4jrw]], [[4tn9]], [[4aqo]], [[2y72]] - ChColG PKD domain<br /> | ||
**[[1nqj]] - ChColG CBD domain <br /> | **[[1nqj]] - ChColG CBD domain <br /> | ||
**[[1nqd]], [[2o8o]], [[4hpk]]- ChColG CBD domain + Ca<br /> | **[[1nqd]], [[2o8o]], [[4hpk]]- ChColG CBD domain + Ca<br /> |
Revision as of 14:38, 14 November 2016
Collagenase (Col) catalyzes the breaking of peptide bonds in collagen. Col cleaves pro-collagen to create collagen. Some collagenases are part of the Matrix metalloproteinase family. RelevanceCol is used for therapy of wounds, Dupuytren's contracture and Peyronie's disease. Structural highlightsClostridium histolycum collagenase contains several domains among them: peptidase domain (residues 331-721), polycystic kidney disease domain (PKD residues 792-880), collagen-binding domain (CBD residues 1003-1118). The peptidase domain contains a , a and an .[1] .
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3D Structures of collagenase3D Structures of collagenase
Updated on 14-November-2016
ReferencesReferences
- ↑ Eckhard U, Schonauer E, Brandstetter H. Structural basis for activity regulation and substrate preference of clostridial collagenases G, H, and T. J Biol Chem. 2013 May 23. PMID:23703618 doi:10.1074/jbc.M112.448548