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6c0v

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<SX load='6c0v' size='340' side='right' viewer='molstar' caption='[[6c0v]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='6c0v' size='340' side='right' viewer='molstar' caption='[[6c0v]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6c0v]] is a 1 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=6C0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C0V FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6c0v]] is a 1 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=6C0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C0V FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ABCB1, MDR1, PGY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Xenobiotic-transporting_ATPase Xenobiotic-transporting ATPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.44 3.6.3.44] </span></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=6c0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c0v OCA], [https://pdbe.org/6c0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c0v RCSB], [https://www.ebi.ac.uk/pdbsum/6c0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c0v ProSAT]</span></td></tr>
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<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=6c0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c0v OCA], [http://pdbe.org/6c0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c0v RCSB], [http://www.ebi.ac.uk/pdbsum/6c0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c0v ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN]] Ulcerative colitis. Disease susceptibility is associated with variations affecting the gene represented in this entry.
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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.
== Function ==
== Function ==
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[[http://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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The multidrug transporter P-glycoprotein is an ATP-binding cassette exporter responsible for clinical resistance to chemotherapy. P-glycoprotein extrudes toxic molecules and drugs from cells through ATP-powered conformational changes. Despite decades of effort, only the structures of the inward-facing conformation of P-glycoprotein are available. Here we present the structure of human P-glycoprotein in the outward-facing conformation, determined by electron cryo-microscopy at 3.4-A resolution. The two nucleotide-binding domains form a closed dimer occluding two ATP molecules. The drug-binding cavity observed in the inward-facing structures is re-orientated toward the extracellular space and compressed to preclude substrate binding. This observation indicates that ATP binding, not hydrolysis, promotes substrate release. The structure evokes a model in which the dynamic nature of P-glycoprotein enables translocation of a large variety of substrates.
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Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation.,Kim Y, Chen J Science. 2018 Jan 25. pii: science.aar7389. doi: 10.1126/science.aar7389. PMID:29371429<ref>PMID:29371429</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 6c0v" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Human]]
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Xenobiotic-transporting ATPase]]
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[[Category: Chen J]]
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[[Category: Chen, J]]
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[[Category: Kim YJ]]
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[[Category: Kim, Y J]]
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[[Category: Abc transporter]]
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[[Category: Abcb1]]
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[[Category: Cryo-em]]
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[[Category: Multidrug resistance]]
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[[Category: P-glycoprotein]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Structural genomic]]
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[[Category: Transport protein]]
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Current revision

Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation

6c0v, resolution 3.40Å

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