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| - | [[Image:1mmr.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mmr| PDB=1mmr | SCENE= }} | | {{STRUCTURE_1mmr| PDB=1mmr | SCENE= }} |
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| - | '''MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR'''
| + | ===MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR=== |
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| - | ==Overview==
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| - | Matrix metalloproteases are a family of enzymes that play critical roles in the physiological and pathological degradation of the extracellular matrix. These enzymes may be important therapeutic targets for the treatment of various diseases where tissue degradation is part of the pathology, such as cancer and arthritis. Matrilysin is the smallest member of this family of enzymes, all of which require zinc for catalytic activity. The first X-ray crystal structures of human matrilysin are presented. Inhibitors of metalloproteases are often characterized by the chemical group that interacts with the active site zinc of the protein. The structures of matrilysin complexed with hydroxamate (maximum resolution 1.9 A), carboxylate (maximum resolution 2.4 A), and sulfodiimine (maximum resolution 2.3 A) inhibitors are presented here and provide detailed information about how each functional group interacts with the catalytic zinc. Only the zinc-coordination group is variable in this series of inhibitors. Examination of these inhibitor-matrilysin complexes emphasizes the dominant role the zinc-coordinating group plays in determining the relative potencies of the inhibitors. The structures of these matrilysin-inhibitor complexes also provide a basis for comparing the catalytic mechanism of MMPs and other metalloproteins.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7756291}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7756291 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7756291}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Smith, W W.]] | | [[Category: Smith, W W.]] |
| | [[Category: Metalloprotease]] | | [[Category: Metalloprotease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:25:57 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 00:23:57 2008'' |
Revision as of 21:24, 2 July 2008
Template:STRUCTURE 1mmr
MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR
Template:ABSTRACT PUBMED 7756291
About this Structure
1MMR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Matrilysin-inhibitor complexes: common themes among metalloproteases., Browner MF, Smith WW, Castelhano AL, Biochemistry. 1995 May 23;34(20):6602-10. PMID:7756291
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