4q9h

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==P-glycoprotein at 3.4 A resolution==
==P-glycoprotein at 3.4 A resolution==
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<StructureSection load='4q9h' size='340' side='right' caption='[[4q9h]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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<StructureSection load='4q9h' size='340' side='right'caption='[[4q9h]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4q9h]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q9H FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4q9h]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q9H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q9H FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4q9i|4q9i]], [[4q9j|4q9j]], [[4q9k|4q9k]], [[4q9l|4q9l]]</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">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</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=4q9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q9h OCA], [https://pdbe.org/4q9h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q9h RCSB], [https://www.ebi.ac.uk/pdbsum/4q9h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q9h 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=4q9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q9h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q9h RCSB], [http://www.ebi.ac.uk/pdbsum/4q9h PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MDR1A_MOUSE MDR1A_MOUSE]] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.<ref>PMID:19325113</ref>
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[https://www.uniprot.org/uniprot/MDR1A_MOUSE MDR1A_MOUSE] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.<ref>PMID:19325113</ref>
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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 a transporter of great clinical and pharmacological significance. Several structural studies of P-gp and its homologs have provided insights into its transport cycle, but questions remain regarding how P-gp recognizes diverse substrates and how substrate binding is coupled to ATP hydrolysis. Here, four new P-gp co-crystal structures with a series of rationally designed ligands are presented. It is observed that the binding of certain ligands, including an ATP-hydrolysis stimulator, produces a large conformational change in the fourth transmembrane helix, which is positioned to potentially transmit a signal to the nucleotide-binding domains. A new ligand-binding site on the surface of P-gp facing the inner leaflet of the membrane is also described, providing vital insights regarding the entry mechanism of hydrophobic drugs and lipids into P-gp. These results represent significant advances in the understanding of how P-gp and related transporters bind and export a plethora of metabolites, antibiotics and clinically approved and pipeline drugs.
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Snapshots of ligand entry, malleable binding and induced helical movement in P-glycoprotein.,Szewczyk P, Tao H, McGrath AP, Villaluz M, Rees SD, Lee SC, Doshi R, Urbatsch IL, Zhang Q, Chang G Acta Crystallogr D Biol Crystallogr. 2015 Mar 1;71(Pt 3):732-41. doi:, 10.1107/S1399004715000978. Epub 2015 Feb 26. PMID:25760620<ref>PMID:25760620</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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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Xenobiotic-transporting ATPase]]
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[[Category: Large Structures]]
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[[Category: Chang, G]]
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[[Category: Mus musculus]]
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[[Category: McGrath, A P]]
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[[Category: Chang G]]
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[[Category: Szewczyk, P]]
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[[Category: McGrath AP]]
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[[Category: Hydrolase]]
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[[Category: Szewczyk P]]
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[[Category: Membrane protein]]
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[[Category: Transporter]]
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Current revision

P-glycoprotein at 3.4 A resolution

PDB ID 4q9h

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