3g5u

<StructureSection load='3g5u' size='340' side='right' caption='[[3g5u]], [[Resolution|resolution]] 3.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[3g5u]] is a 2 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=3G5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G5U FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3g60|3g60]], [[3g61|3g61]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Abcb1a, mCG_1178 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g5u OCA], [http://pdbe.org/3g5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g5u RCSB], [http://www.ebi.ac.uk/pdbsum/3g5u PDBsum]</span></td></tr>

[[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>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/g5/3g5u_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

P-glycoprotein (P-gp) detoxifies cells by exporting hundreds of chemically unrelated toxins but has been implicated in multidrug resistance (MDR) in the treatment of cancers. Substrate promiscuity is a hallmark of P-gp activity, thus a structural description of poly-specific drug-binding is important for the rational design of anticancer drugs and MDR inhibitors. The x-ray structure of apo P-gp at 3.8 angstroms reveals an internal cavity of approximately 6000 angstroms cubed with a 30 angstrom separation of the two nucleotide-binding domains. Two additional P-gp structures with cyclic peptide inhibitors demonstrate distinct drug-binding sites in the internal cavity capable of stereoselectivity that is based on hydrophobic and aromatic interactions. Apo and drug-bound P-gp structures have portals open to the cytoplasm and the inner leaflet of the lipid bilayer for drug entry. The inward-facing conformation represents an initial stage of the transport cycle that is competent for drug binding.

Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding.,Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, Zhuo R, Harrell PM, Trinh YT, Zhang Q, Urbatsch IL, Chang G Science. 2009 Mar 27;323(5922):1718-22. PMID:19325113<ref>PMID:19325113</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3g5u" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Aller, S G]]

[[Category: Chang, G]]

[[Category: Chittaboina, S]]

[[Category: Harrell, P M]]

[[Category: Trinh, Y T]]

[[Category: Urbatsch, I L]]

[[Category: Ward, A]]

[[Category: Weng, Y]]

[[Category: Yu, J]]

[[Category: Zhang, Q]]

[[Category: Zhuo, R]]

[[Category: Pgp]]