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[[Image:1kbc.jpg|left|200px]]<br /><applet load="1kbc" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1kbc, resolution 1.8&Aring;" />
'''PROCARBOXYPEPTIDASE TERNARY COMPLEX'''<br />


==Overview==
==PROCARBOXYPEPTIDASE TERNARY COMPLEX==
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.
<StructureSection load='1kbc' size='340' side='right'caption='[[1kbc]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>


==About this Structure==
==See Also==
1KBC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=HLE:'>HLE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KBC OCA].
*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=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 Fri Feb 15 16:12:14 2008''

Latest revision as of 10:45, 7 February 2024

PROCARBOXYPEPTIDASE TERNARY COMPLEXPROCARBOXYPEPTIDASE TERNARY COMPLEX

Structural highlights

1kbc is a 2 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 1.8Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MMP8_HUMAN Can degrade fibrillar type I, II, and III collagens.

Evolutionary Conservation

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

See Also

1kbc, resolution 1.80Å

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