8y6h

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Current revision (07:48, 21 November 2024) (edit) (undo)
 
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<table><tr><td colspan='2'>[[8y6h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Y6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y6H FirstGlance]. <br>
<table><tr><td colspan='2'>[[8y6h]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8Y6H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8Y6H FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.49&#8491;</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.49&#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=R0Z:elacridar'>R0Z</scene></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=R0Z:~{N}-[4-[2-(6,7-dimethoxy-3,4-dihydro-1~{H}-isoquinolin-2-yl)ethyl]phenyl]-5-methoxy-9-oxidanylidene-10~{H}-acridine-4-carboxamide'>R0Z</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8y6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y6h OCA], [https://pdbe.org/8y6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y6h RCSB], [https://www.ebi.ac.uk/pdbsum/8y6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y6h ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8y6h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8y6h OCA], [https://pdbe.org/8y6h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8y6h RCSB], [https://www.ebi.ac.uk/pdbsum/8y6h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8y6h ProSAT]</span></td></tr>
</table>
</table>
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[https://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN] Ulcerative colitis. Disease susceptibility is associated with variations affecting the gene represented in this entry.
[https://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN] Ulcerative colitis. Disease susceptibility is associated with variations affecting the gene represented in this entry.
== Function ==
== Function ==
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[https://www.uniprot.org/uniprot/A0A1S4NYF2_BRALA A0A1S4NYF2_BRALA] [https://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
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[https://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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P-glycoprotein (P-gp) is an ATP-binding cassette transporter known for its roles in expelling xenobiotic compounds from cells and contributing to cellular drug resistance through multidrug efflux. This mechanism is particularly problematic in cancer cells, where it diminishes the therapeutic efficacy of anticancer drugs. P-gp inhibitors, such as elacridar, have been developed to circumvent the decrease in drug efficacy due to P-gp efflux. An earlier study reported the cryo-EM structure of human P-gp-Fab (MRK-16) complex bound by two elacridar molecules, at a resolution of 3.6 A. In this study, we have obtained a higher resolution (2.5 A) structure of the P-gp- Fab (UIC2) complex bound by three elacridar molecules. This finding, which exposes a larger space for compound-binding sites than previously acknowledged, has significant implications for the development of more selective inhibitors and enhances our understanding of the compound recognition mechanism of P-gp.
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Cryo-EM structure of P-glycoprotein bound to triple elacridar inhibitor molecules.,Hamaguchi-Suzuki N, Adachi N, Moriya T, Yasuda S, Kawasaki M, Suzuki K, Ogasawara S, Anzai N, Senda T, Murata T Biochem Biophys Res Commun. 2024 May 21;709:149855. doi: , 10.1016/j.bbrc.2024.149855. Epub 2024 Mar 28. PMID:38579618<ref>PMID:38579618</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 8y6h" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

P-glycoprotein in complex with UIC2 Fab and triple elacridar molecules in LMNG detergent

PDB ID 8y6h

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