6a72

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'''Unreleased structure'''
 
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The entry 6a72 is ON HOLD until Paper Publication
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==Copper transporter protein==
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<StructureSection load='6a72' size='340' side='right'caption='[[6a72]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6a72]] 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=6A72 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A72 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=9UX:dioxo(di-mu-sulfide)dimolybdenum'>9UX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=6a72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a72 OCA], [https://pdbe.org/6a72 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a72 RCSB], [https://www.ebi.ac.uk/pdbsum/6a72 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a72 ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/ATP7B_HUMAN ATP7B_HUMAN] Defects in ATP7B are the cause of Wilson disease (WD) [MIM:[https://omim.org/entry/277900 277900]. WD is an autosomal recessive disorder of copper metabolism in which copper cannot be incorporated into ceruloplasmin in liver, and cannot be excreted from the liver into the bile. Copper accumulates in the liver and subsequently in the brain and kidney. The disease is characterized by neurologic manifestations and signs of cirrhosis.<ref>PMID:8298641</ref> <ref>PMID:7626145</ref> <ref>PMID:8533760</ref> <ref>PMID:8938442</ref> <ref>PMID:8931691</ref> <ref>PMID:8782057</ref> <ref>PMID:9311736</ref> <ref>PMID:9772425</ref> <ref>PMID:9222767</ref> <ref>PMID:8980283</ref> <ref>PMID:9887381</ref> <ref>PMID:9482578</ref> <ref>PMID:9554743</ref> <ref>PMID:9452121</ref> <ref>PMID:9671269</ref> <ref>PMID:9829905</ref> <ref>PMID:10194254</ref> <ref>PMID:10447265</ref> <ref>PMID:10502776</ref> <ref>PMID:10502777</ref> <ref>PMID:10051024</ref> <ref>PMID:10544227</ref> <ref>PMID:10453196</ref> <ref>PMID:11216666</ref> <ref>PMID:11093740</ref> <ref>PMID:10790207</ref> <ref>PMID:10721669</ref> <ref>PMID:11043508</ref> <ref>PMID:11180609</ref> <ref>PMID:11690702</ref> <ref>PMID:11243728</ref> <ref>PMID:11954751</ref> <ref>PMID:12544487</ref> <ref>PMID:12325021</ref> <ref>PMID:12376745</ref> <ref>PMID:14986826</ref> <ref>PMID:14639035</ref> <ref>PMID:15024742</ref> <ref>PMID:15557537</ref> <ref>PMID:14966923</ref> <ref>PMID:15845031</ref> <ref>PMID:15811015</ref> <ref>PMID:15952988</ref> <ref>PMID:16207219</ref> <ref>PMID:16283883</ref> <ref>PMID:16088907</ref> <ref>PMID:15967699</ref> <ref>PMID:17718866</ref> <ref>PMID:18373411</ref> <ref>PMID:18203200</ref> <ref>PMID:21682854</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/ATP7B_HUMAN ATP7B_HUMAN] Involved in the export of copper out of the cells, such as the efflux of hepatic copper into the bile.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tetrathiomolybdate (TM) is used in the clinic for the treatment of Wilson's disease by targeting the cellular copper efflux protein ATP7B (WLN). Interestingly, both TM and WLN are associated with the efficacy of cisplatin, a widely used anticancer drug. Herein, we show that TM induces dimerization of the metal-binding domain of ATP7B (WLN4) through a unique sulfur-bridged Mo2S6O2 cluster. TM expels copper ions from Cu-WLN4 and forms a copper-free dimer. The binding of Mo to cysteine residues of WLN4 inhibits platination of the protein. Reaction with multi-domain proteins indicates that TM can also connect two domains in the same molecule, forming Mo-bridged intramolecular crosslinks. These results provide structural and chemical insight into the mechanism of action of TM against ATPase, and reveal the molecular mechanism by which TM attenuates the cisplatin resistance mediated by copper efflux proteins.
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Authors:
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Tetrathiomolybdate induces dimerization of the metal-binding domain of ATPase and inhibits platination of the protein.,Fang T, Chen W, Sheng Y, Yuan S, Tang Q, Li G, Huang G, Su J, Zhang X, Zang J, Liu Y Nat Commun. 2019 Jan 14;10(1):186. doi: 10.1038/s41467-018-08102-z. PMID:30643139<ref>PMID:30643139</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6a72" style="background-color:#fffaf0;"></div>
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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: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Chen WB]]

Current revision

Copper transporter protein

PDB ID 6a72

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