6a72
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Copper transporter protein== | |
| + | <StructureSection load='6a72' size='340' side='right'caption='[[6a72]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6a72]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A72 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9UX:dioxo(di-mu-sulfide)dimolybdenum'>9UX</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=6a72 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a72 OCA], [http://pdbe.org/6a72 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a72 RCSB], [http://www.ebi.ac.uk/pdbsum/6a72 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a72 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6a72" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Chen, W B]] | ||
| + | [[Category: Copper transporter protein]] | ||
| + | [[Category: Metal transport]] | ||
Revision as of 06:50, 3 April 2019
Copper transporter protein
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