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


{{Structure
==MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR==
|PDB= 1mmr |SIZE=350|CAPTION= <scene name='initialview01'>1mmr</scene>, resolution 2.4&Aring;
<StructureSection load='1mmr' size='340' side='right'caption='[[1mmr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<table><tr><td colspan='2'>[[1mmr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MMR FirstGlance]. <br>
|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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mmr OCA], [https://pdbe.org/1mmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mmr RCSB], [https://www.ebi.ac.uk/pdbsum/1mmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mmr ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/MMP7_HUMAN MMP7_HUMAN] Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.<ref>PMID:2550050</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mm/1mmr_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mmr ConSurf].
<div style="clear:both"></div>


'''MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR'''
==See Also==
 
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1MMR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MMR OCA].
 
==Reference==
Matrilysin-inhibitor complexes: common themes among metalloproteases., Browner MF, Smith WW, Castelhano AL, Biochemistry. 1995 May 23;34(20):6602-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7756291 7756291]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Matrilysin]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Browner MF]]
[[Category: Browner, M F.]]
[[Category: Castelhano AL]]
[[Category: Castelhano, A L.]]
[[Category: Smith WW]]
[[Category: Smith, W W.]]
[[Category: metalloprotease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:18:09 2008''

Latest revision as of 10:45, 14 February 2024

MATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITORMATRILYSIN COMPLEXED WITH SULFODIIMINE INHIBITOR

Structural highlights

1mmr is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MMP7_HUMAN Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase.[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

References

  1. ↑ Quantin B, Murphy G, Breathnach R. Pump-1 cDNA codes for a protein with characteristics similar to those of classical collagenase family members. Biochemistry. 1989 Jun 27;28(13):5327-34. PMID:2550050

1mmr, resolution 2.40Å

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