Collagenase (non-MMP): Difference between revisions

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== 3D Structures of collagenase ==
[[Collagenase 3D structures]]
</StructureSection>
</StructureSection>
== 3D Structures of collagenase ==
== 3D Structures of collagenase ==
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**[[4ar1]] – ChColH  peptidase domain <br />
**[[4ar1]] – ChColH  peptidase domain <br />
**[[4arf]] – CtColH  peptidase domain + peptide inhibitor <br />
**[[4arf]] – CtColH  peptidase domain + peptide inhibitor <br />
**[[5o7e]] – ColH  peptidase domain + inhibitor – ''Hathewaya histolytica''<br />


*Collagenase T
*Collagenase T
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**[[1hyl]], [[2hlc]] – Col – ''Hypoderma lineatum''<br />
**[[1hyl]], [[2hlc]] – Col – ''Hypoderma lineatum''<br />
**[[5sv5]] – Col C-terminal – ''Bacillus anthracis''<br />
**[[5sv5]] – Col C-terminal – ''Bacillus anthracis''<br />
*Collagenase 3 or matrix metalloproteinase 13 see [[Matrix metalloproteinase]]
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== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 12:27, 14 May 2019


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] Water molecules are shown as red spheres. .


3D Structures of collagenase

Collagenase 3D structures


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 14-May-2019

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