6c0v
From Proteopedia
(Difference between revisions)
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<StructureSection load='6c0v' size='340' side='right' caption='[[6c0v]], [[Resolution|resolution]] 3.40Å' scene=''> | <StructureSection load='6c0v' size='340' side='right' caption='[[6c0v]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[6c0v]] is a 1 chain structure. 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> | + | <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> |
</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> | </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> | ||
| + | <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> | ||
<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> | <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> | ||
<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> | <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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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN]] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. | [[http://www.uniprot.org/uniprot/MDR1_HUMAN MDR1_HUMAN]] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6c0v" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Xenobiotic-transporting ATPase]] | [[Category: Xenobiotic-transporting ATPase]] | ||
[[Category: Chen, J]] | [[Category: Chen, J]] | ||
Revision as of 06:48, 7 February 2018
Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation
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