Collagenase (non-MMP): Difference between revisions

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**[[4jrw]], [[4tn9]], [[4aqo]], [[2y72]] - ChColG PKD domain<br />
**[[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]], [[5iku]] - ChColG CBD domain + Ca<br />


*Collagenase H
*Collagenase H

Revision as of 12:10, 12 April 2018


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.

Relevance

Col is used for therapy of wounds, Dupuytren's contracture and Peyronie's disease.

Structural highlights

Clostridium 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] .


Collagenase H peptidase domain (cyan) complex with peptidic inhibitor, isopentenyl phosphate, Ca+2 (green) and Zn+2 (grey) ions (PDB entry 4arf)

Drag the structure with the mouse to rotate

3D Structures of collagenase3D Structures of collagenase

Updated on 12-April-2018

ReferencesReferences

  1. 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

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky