1kbc: Difference between revisions

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OCA

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-[[Image:1kbc.gif|left|200px]]<br />
-<applet load="1kbc" size="450" 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==
-KBC 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 CA, ZN and HLE 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KBC OCA].
+*[[Matrix metalloproteinase 3D structures|Matrix metalloproteinase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-.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: 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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:49:38 2007''