1mmr: Difference between revisions

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[[Image:1mmr.gif|left|200px]]
[[Image:1mmr.gif|left|200px]]


{{Structure
<!--
|PDB= 1mmr |SIZE=350|CAPTION= <scene name='initialview01'>1mmr</scene>, resolution 2.4&Aring;
The line below this paragraph, containing "STRUCTURE_1mmr", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SRS:4-METHYL-3-(9-OXO-1,8-DIAZA-TRICYCLO[10.6.1.0(13,18)]NONADECA-12(19),13(18),15,17-TETRAENE-10-CARBAMOYL)PENTA-METHYLSULFONEDIIMINE'>SRS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Matrilysin Matrilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.23 3.4.24.23] </span>
or leave the SCENE parameter empty for the default display.
|GENE=  
-->
|DOMAIN=
{{STRUCTURE_1mmr| PDB=1mmr  | SCENE= }}  
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmr OCA], [http://www.ebi.ac.uk/pdbsum/1mmr PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mmr RCSB]</span>
}}


'''MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR'''
'''MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR'''
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[[Category: Castelhano, A L.]]
[[Category: Castelhano, A L.]]
[[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 Sun Mar 30 22:18:09 2008''

Revision as of 01:25, 3 May 2008

File:1mmr.gif

Template:STRUCTURE 1mmr

MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR


OverviewOverview

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.

About this StructureAbout this Structure

1MMR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Matrilysin-inhibitor complexes: common themes among metalloproteases., Browner MF, Smith WW, Castelhano AL, Biochemistry. 1995 May 23;34(20):6602-10. PMID:7756291 Page seeded by OCA on Sat May 3 01:25:57 2008

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