5wdj

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<StructureSection load='5wdj' size='340' side='right' caption='[[5wdj]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='5wdj' size='340' side='right' caption='[[5wdj]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5wdj]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WDJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5wdj]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WDJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AEY:7-(benzyloxy)-1H-[1,2,3]triazolo[4,5-d]pyrimidin-5-amine'>AEY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AEY:7-(benzyloxy)-1H-[1,2,3]triazolo[4,5-d]pyrimidin-5-amine'>AEY</scene>, <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MPO ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Myeloperoxidase Myeloperoxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.2.2 1.11.2.2] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Myeloperoxidase Myeloperoxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.2.2 1.11.2.2] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wdj OCA], [http://pdbe.org/5wdj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wdj RCSB], [http://www.ebi.ac.uk/pdbsum/5wdj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wdj ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5wdj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wdj OCA], [http://pdbe.org/5wdj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wdj RCSB], [http://www.ebi.ac.uk/pdbsum/5wdj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wdj ProSAT]</span></td></tr>
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== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PERM_HUMAN PERM_HUMAN]] Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
[[http://www.uniprot.org/uniprot/PERM_HUMAN PERM_HUMAN]] Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Myeloperoxidase, a mammalian peroxidase involved in the immune system as an anti-microbial first responder, can produce hypochlorous acid in response to invading pathogens. Myeloperoxidase has been implicated in several chronic pathological diseases due to the chronic production of hypochlorous acid, as well as other reactive radical species. A high throughput screen and triaging protocol was developed to identify a reversible inhibitor of myeloperoxidase toward the potential treatment of chronic diseases such as atherosclerosis. The identification and characterization of a reversible myeloperoxidase inhibitor, 7-(benzyloxy)-3H-[1,2,3]triazolo[4,5-d]pyrimidin-5-amine is described.
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Triazolopyrimidines identified as reversible myeloperoxidase inhibitors.,Duclos F, Abell LM, Harden DG, Pike K, Nowak K, Locke GA, Duke GJ, Liu X, Fernando G, Shaw SA, Vokits BP, Wurtz NR, Viet A, Valente MN, Stachura S, Sleph P, Khan JA, Gao J, Dongre AR, Zhao L, Wexler RR, Gordon DA, Kick EK Medchemcomm. 2017 Oct 26;8(11):2093-2099. doi: 10.1039/c7md00268h. eCollection, 2017 Nov 1. PMID:30108726<ref>PMID:30108726</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5wdj" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Myeloperoxidase|Myeloperoxidase]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
[[Category: Myeloperoxidase]]
[[Category: Myeloperoxidase]]
[[Category: Khan, J A]]
[[Category: Khan, J A]]
[[Category: Metal binding protein]]
[[Category: Metal binding protein]]

Revision as of 07:07, 31 October 2018

CRYSTAL STRUCTURE OF MYELOPEROXIDASE SUBFORM C (MPO) COMPLEX WITH COMPOUND-6 AKA 7-(BENZYLOXY)-1H-[1,2, 3]TRIAZOLO[4,5-D]PYRIMIDIN-5-AMINE

5wdj, resolution 2.40Å

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