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8pch

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(New page: 200px<br /> <applet load="8pch" size="450" color="white" frame="true" align="right" spinBox="true" caption="8pch, resolution 2.1&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:8pch.gif|left|200px]]<br />
 
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<applet load="8pch" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="8pch, resolution 2.1&Aring;" />
 
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'''CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION==
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BACKGROUND: Cathepsin H is a lysosomal cysteine protease, involved in, intracellular protein degradation. It is the only known, mono-aminopeptidase in the papain-like family and is reported to be, involved in tumor metastasis. The cathepsin H structure was determined in, order to investigate the structural basis for its aminopeptidase activity, and thus to provide the basis for structure-based design of synthetic, inhibitors. RESULTS: The crystal structure of native porcine cathepsin H, was determined at 2.1 A resolution. The structure has the typical, papain-family fold. The so-called mini-chain, the octapeptide EPQNCSAT, is, attached via a disulfide bond to the body of the enzyme and bound in a, narrowed active-site cleft, in the substrate-binding direction. The, mini-chain fills the ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9493267 (full description)]]
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<StructureSection load='8pch' size='340' side='right'caption='[[8pch]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[8pch]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8PCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8PCH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8pch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8pch OCA], [https://pdbe.org/8pch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8pch RCSB], [https://www.ebi.ac.uk/pdbsum/8pch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8pch ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CATH_PIG CATH_PIG]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pc/8pch_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=8pch ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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BACKGROUND: Cathepsin H is a lysosomal cysteine protease, involved in intracellular protein degradation. It is the only known mono-aminopeptidase in the papain-like family and is reported to be involved in tumor metastasis. The cathepsin H structure was determined in order to investigate the structural basis for its aminopeptidase activity and thus to provide the basis for structure-based design of synthetic inhibitors. RESULTS: The crystal structure of native porcine cathepsin H was determined at 2.1 A resolution. The structure has the typical papain-family fold. The so-called mini-chain, the octapeptide EPQNCSAT, is attached via a disulfide bond to the body of the enzyme and bound in a narrowed active-site cleft, in the substrate-binding direction. The mini-chain fills the region that in related enzymes comprises the non-primed substrate-binding sites from S2 backwards. CONCLUSIONS: The crystal structure of cathepsin H reveals that the mini-chain has a definitive role in substrate recognition and that carbohydrate residues attached to the body of the enzyme are involved in positioning the mini-chain in the active-site cleft. Modeling of a substrate into the active-site cleft suggests that the negatively charged carboxyl group of the C terminus of the mini-chain acts as an anchor for the positively charged N-terminal amino group of a substrate. The observed displacements of the residues within the active-site cleft from their equivalent positions in the papain-like endopeptidases suggest that they form the structural basis for the positioning of both the mini-chain and the substrate, resulting in exopeptidase activity.
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==About this Structure==
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Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.,Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D Structure. 1998 Jan 15;6(1):51-61. PMID:9493267<ref>PMID:9493267</ref>
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8PCH is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.16 3.4.22.16]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=8PCH OCA]].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function., Guncar G, Podobnik M, Pungercar J, Strukelj B, Turk V, Turk D, Structure. 1998 Jan 15;6(1):51-61. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9493267 9493267]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 8pch" style="background-color:#fffaf0;"></div>
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[[Category: Sus scrofa]]
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[[Category: Guncar, G.]]
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[[Category: Podobnik, M.]]
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[[Category: Pungercar, J.]]
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[[Category: Strukelj, B.]]
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[[Category: Turk, D.]]
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[[Category: Turk, V.]]
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[[Category: aminopeptidase]]
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[[Category: cysteine proteinase]]
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[[Category: hydrolase]]
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[[Category: protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 15:59:45 2007''
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==See Also==
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*[[Cathepsin 3D structures|Cathepsin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Sus scrofa]]
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[[Category: Guncar G]]
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[[Category: Podobnik M]]
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[[Category: Pungercar J]]
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[[Category: Strukelj B]]
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[[Category: Turk D]]
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[[Category: Turk V]]

Current revision

CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION

PDB ID 8pch

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