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4q9l
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==P-glycoprotein cocrystallised with QZ-Phe== | |
| + | <StructureSection load='4q9l' size='340' side='right'caption='[[4q9l]], [[Resolution|resolution]] 3.80Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4q9l]] is a 3 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=4Q9L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q9L FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=30F:(2Z)-2-AMINO-3-SELANYLPROP-2-ENOIC+ACID'>30F</scene>, <scene name='pdbligand=PRD_001233:cyclic-tris-phenylselenazole'>PRD_001233</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=4q9l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q9l OCA], [https://pdbe.org/4q9l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q9l RCSB], [https://www.ebi.ac.uk/pdbsum/4q9l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q9l ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4q9l" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Chang G]] | ||
| + | [[Category: McGrath AP]] | ||
| + | [[Category: Szewczyk P]] | ||
Current revision
P-glycoprotein cocrystallised with QZ-Phe
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