3mph

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[[Image:3mph.png|left|200px]]
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==The structure of human diamine oxidase complexed with an inhibitor aminoguanidine==
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<StructureSection load='3mph' size='340' side='right' caption='[[3mph]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3mph]] is a 2 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=3MPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MPH FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
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<tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=AGQ:3-[(3E)-3-(CARBAMIMIDOYLHYDRAZONO)-4-HYDROXY-6-OXOCYCLOHEXA-1,4-DIEN-1-YL]-L-ALANINE'>AGQ</scene></td></tr>
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<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hi7|3hi7]], [[3hig|3hig]], [[3hii|3hii]], [[3k5t|3k5t]]</td></tr>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Diamine_oxidase Diamine oxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.4.3.22 1.4.3.22] </span></td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3mph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mph RCSB], [http://www.ebi.ac.uk/pdbsum/3mph PDBsum]</span></td></tr>
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<table>
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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/mp/3mph_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/chain_selection.php?pdb_ID=2ata 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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Copper-containing amine oxidases (CAOs) require a protein-derived topaquinone cofactor (TPQ) for activity. TPQ biogenesis is a self-processing reaction requiring the presence of copper and molecular oxygen. Recombinant human diamine oxidase (hDAO) was heterologously expressed in Drosophila S2 cells, and analysis indicates that the purified hDAO contains substoichiometric amounts of copper and TPQ. The crystal structure of a complex of an inhibitor, aminoguanidine, and hDAO at 2.05 A resolution shows that the aminoguanidine forms a covalent adduct with the TPQ and that the site is approximately 75% occupied. Aminoguanidine is a potent inhibitor of hDAO with an IC(50) of 153 +/- 9 nM. The structure indicates that the catalytic metal site, normally occupied by copper, is fully occupied. X-ray diffraction data recorded below the copper edge, between the copper and zinc edges, and above the zinc edge have been used to show that the metal site is occupied approximately 75% by copper and 25% by zinc and the formation of the TPQ cofactor is correlated with copper occupancy.
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Correlation of Active Site Metal Content in Human Diamine Oxidase with Trihydroxyphenylalanine Quinone Cofactor Biogenesis .,McGrath AP, Caradoc-Davies T, Collyer CA, Guss JM Biochemistry. 2010 Sep 1. PMID:20722416<ref>PMID:20722416</ref>
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The line below this paragraph, containing "STRUCTURE_3mph", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_3mph| PDB=3mph | SCENE= }}
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===The structure of human diamine oxidase complexed with an inhibitor aminoguanidine===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<!--
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<references/>
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The line below this paragraph, {{ABSTRACT_PUBMED_20722416}}, adds the Publication Abstract to the page
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__TOC__
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(as it appears on PubMed at http://www.pubmed.gov), where 20722416 is the PubMed ID number.
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</StructureSection>
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{{ABSTRACT_PUBMED_20722416}}
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==About this Structure==
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[[3mph]] is a 2 chain structure with 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=3MPH OCA].
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==Reference==
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<ref group="xtra">PMID:020722416</ref><references group="xtra"/>
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[[Category: Diamine oxidase]]
[[Category: Diamine oxidase]]
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[[Category: Homo sapiens]]
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[[Category: Human]]
[[Category: Guss, J M.]]
[[Category: Guss, J M.]]
[[Category: McGrath, A P.]]
[[Category: McGrath, A P.]]

Revision as of 13:10, 18 May 2014

The structure of human diamine oxidase complexed with an inhibitor aminoguanidine

3mph, resolution 2.05Å

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OCA

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