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4ksb

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Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain

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 ==Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain==
-<StructureSection load='4ksb' size='340' side='right' caption='[[4ksb]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
+<StructureSection load='4ksb' size='340' side='right'caption='[[4ksb]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4ksb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KSB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4KSB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4ksb]] 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=4KSB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KSB FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ksc|4ksc]], [[4ksd|4ksd]], [[4lsg|4lsg]]</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8001&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Abcb1a, Abcb4, Mdr1a, Mdr3, Pgy-3, Pgy3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=4ksb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ksb OCA], [https://pdbe.org/4ksb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ksb RCSB], [https://www.ebi.ac.uk/pdbsum/4ksb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ksb ProSAT]</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=4ksb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ksb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ksb RCSB], [http://www.ebi.ac.uk/pdbsum/4ksb PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[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>
+[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 one of the best-known mediators of drug efflux-based multidrug resistance in many cancers. This validated therapeutic target is a prototypic, plasma membrane resident ATP-Binding Cassette transporter that pumps xenobiotic compounds out of cells. The large, polyspecific drug-binding pocket of P-gp recognizes a variety of structurally unrelated compounds. The transport of these drugs across the membrane is coincident with changes in the size and shape of this pocket during the course of the transport cycle. Here, we present the crystal structures of three inward-facing conformations of mouse P-gp derived from two different crystal forms. One structure has a nanobody bound to the C-terminal side of the first nucleotide-binding domain. This nanobody strongly inhibits the ATP hydrolysis activity of mouse P-gp by hindering the formation of a dimeric complex between the ATP-binding domains, which is essential for nucleotide hydrolysis. Together, these inward-facing conformational snapshots of P-gp demonstrate a range of flexibility exhibited by this transporter, which is likely an essential feature for the binding and transport of large, diverse substrates. The nanobody-bound structure also reveals a unique epitope on P-gp.
-Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain.,Ward AB, Szewczyk P, Grimard V, Lee CW, Martinez L, Doshi R, Caya A, Villaluz M, Pardon E, Cregger C, Swartz DJ, Falson PG, Urbatsch IL, Govaerts C, Steyaert J, Chang G Proc Natl Acad Sci U S A. 2013 Aug 13;110(33):13386-91. doi:, 10.1073/pnas.1309275110. Epub 2013 Jul 30. PMID:23901103<ref>PMID:23901103</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Xenobiotic-transporting ATPase]]
+[[Category: Mus musculus]]
-[[Category: Caya, A]]
+[[Category: Caya A]]
-[[Category: Chang, G]]
+[[Category: Chang G]]
-[[Category: Cregger, C]]
+[[Category: Cregger C]]
-[[Category: Doshi, R]]
+[[Category: Doshi R]]
-[[Category: Falson, P]]
+[[Category: Falson P]]
-[[Category: Govaerts, C]]
+[[Category: Govaerts C]]
-[[Category: Grimard, V]]
+[[Category: Grimard V]]
-[[Category: Lee, C W]]
+[[Category: Lee C-W]]
-[[Category: Martinez, L]]
+[[Category: Martinez L]]
-[[Category: Pardon, E]]
+[[Category: Pardon E]]
-[[Category: Steyaert, J]]
+[[Category: Steyaert J]]
-[[Category: Swartz, D J]]
+[[Category: Swartz DJ]]
-[[Category: Szewczyk, P]]
+[[Category: Szewczyk P]]
-[[Category: Urbatsch, I]]
+[[Category: Urbatsch I]]
-[[Category: Villaluz, M]]
+[[Category: Villaluz M]]
-[[Category: Ward, A]]
+[[Category: Ward A]]
-[[Category: Atp binding]]
-[[Category: Membrane]]
-[[Category: Membrane protein]]
-[[Category: Transport protein]]
-[[Category: Transporter]]

4ksb

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Structures of P-glycoprotein reveal its conformational flexibility and an epitope on the nucleotide-binding domain

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