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[[Image:1kbc.jpg|left|200px]]


{{Structure
==PROCARBOXYPEPTIDASE TERNARY COMPLEX==
|PDB= 1kbc |SIZE=350|CAPTION= <scene name='initialview01'>1kbc</scene>, resolution 1.8&Aring;
<StructureSection load='1kbc' size='340' side='right'caption='[[1kbc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=HLE:3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC ACID HYDROXYAMIDE'>HLE</scene>
<table><tr><td colspan='2'>[[1kbc]] is a 2 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=1KBC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KBC FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#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=HLE:3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC+ACID+HYDROXYAMIDE'>HLE</scene>, <scene name='pdbligand=RIN:3-AMINO-AZACYCLOTRIDECAN-2-ONE'>RIN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
}}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kbc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kbc OCA], [https://pdbe.org/1kbc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kbc RCSB], [https://www.ebi.ac.uk/pdbsum/1kbc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kbc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MMP8_HUMAN MMP8_HUMAN] Can degrade fibrillar type I, II, and III collagens.
== 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/kb/1kbc_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=1kbc ConSurf].
<div style="clear:both"></div>


'''PROCARBOXYPEPTIDASE TERNARY COMPLEX'''
==See Also==
 
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Matrix metalloproteinases (MMP) are zinc endopeptidases involved in tissue remodelling. They have been implicated in a series of pathologies, including cancer, arthritis, joint destruction and Alzheimer's disease. Human neutrophil collagenase represents one of the three interstitial collagenases that cleave triple-helical collagen of type I, II and III. Its catalytic domain (residues Phe79-Gly242) has been heterologously expressed in Escherichia coli and crystallized as a non-covalent complex with the hydroxamate inhibitor BB-1909, which has distinct selectivity against different MMP, in a crystal form. The crystal structure, refined to 0.18-nm resolution, shows that BB-1909 is a right-hand-side inhibitor that binds to the S1'-S3' subsites and coordinates to the catalytic Zn2+ in a bidentate manner via the hydroxyl and carbonyl oxygen atoms of the hydroxamate group in a similar manner to batimastat. The collagenase/BB-1909 complex is described in detail and compared with the collagenase/batimastat complex. These studies provide information on MMP specificity and thus may assist the development of more-selective MMP inhibitors.
 
==About this Structure==
1KBC 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=1KBC OCA].
 
==Reference==
1.8-A crystal structure of the catalytic domain of human neutrophil collagenase (matrix metalloproteinase-8) complexed with a peptidomimetic hydroxamate primed-side inhibitor with a distinct selectivity profile., Betz M, Huxley P, Davies SJ, Mushtaq Y, Pieper M, Tschesche H, Bode W, Gomis-Ruth FX, Eur J Biochem. 1997 Jul 1;247(1):356-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9249047 9249047]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Neutrophil collagenase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Betz M]]
[[Category: Betz, M.]]
[[Category: Bode W]]
[[Category: Bode, W.]]
[[Category: Gomis-Rueth FX]]
[[Category: Gomis-Rueth, F X.]]
[[Category: CA]]
[[Category: HLE]]
[[Category: ZN]]
[[Category: collagenase]]
[[Category: hnc]]
[[Category: hydrolase]]
[[Category: hydrolytic enzyme]]
[[Category: inhibitor]]
[[Category: matrixin]]
[[Category: metalloproteinase]]
[[Category: mmp-8]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:15:06 2008''

Latest revision as of 07:45, 7 February 2024

PROCARBOXYPEPTIDASE TERNARY COMPLEX

1kbc, resolution 1.80Å

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