Sandbox 985
From Proteopedia
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== Function == | == Function == | ||
- | + | MMP-9 is absent from most normal adult tissues, including the intestinal epithelial cells. We and several others have shown that MMP-9 is highly expressed during intestinal inflammation in different animal models and human IBD. In addition to its role in inflammation, recent studies from our laboratory have shown that MMP-9 plays a role in epithelial cell differentiation. | |
== Disease == | == Disease == | ||
Revision as of 02:44, 4 May 2015
MMP family members share similar fundamental structural characteristics and are classified according to their substrate specificity. By this classification, MMP-9 belongs to the gelatinase subgroup and is known as gelatinase B due to its ability to degrade gelatin. MMP9 is composed of the following domains: a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. The zinc binding motif HEXXHXXGXXH in the catalytic domain, and the “cysteine switch” motif PRCGXPD in the propeptide are common structural signatures, where three histidines in the zinc binding motif coordinate and the cysteine in the propetide coordinate with the catalytic zinc ion. MMP9 is produced by the several cell types, normal alveolar macrophages and granulocytes.
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References
- ↑ Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
- ↑ Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644