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==== Catalytic domain ====
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It seems to have 163 residues involved in the catalytic domain: Met80-Gly242.
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(http://www.ncbi.nlm.nih.gov/pmc/articles/PMC394940/?page=1). The catalytic zinc ion is situated at the bottom of the active-site. The other zinc ion and the two calcium ions are packed against the top of the beta sheet and presumably function to stabilize the catalytic domain. The polypeptide folding and in particular the zinc environment of the collagenase catalytic domain bear a close ressemblance to the astacins and the snake venom metalloproteinases.

Revision as of 20:32, 27 January 2016

MMP8

Is enzyme : EC=3.4.24.34 => Hydrolase Called Neutrophil collagenase. zinc-dependent and calcium-dependent proteases that degrade most components of the extracellular matrix

Caption for this structure

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References

  1. "MMP8 matrix metallopeptidase 8 (neutrophil collagenase)"
  2. Stams T, Spurlino JC, Smith DL, Wahl RC, Ho TF, Qoronfleh MW, Banks TM, Rubin B. Structure of human neutrophil collagenase reveals large S1' specificity pocket. Nat Struct Biol. 1994 Feb;1(2):119-23. PMID:7656015
  3. "Neutrophil collagenase"
  4. "Metalloendopeptidase activity"


TEST:

RESSOURCE : Image:2oy4 mm1.pdb ( la structure du monomère )

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