6hzm

From Proteopedia

(Difference between revisions)

Revision as of 08:21, 14 November 2018

Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)

Structural highlights

6hzm is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	6hbu
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[ABCG2_HUMAN] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.^[1] ^[2] ^[3] ^[4]

References

↑ Zhang W, Mojsilovic-Petrovic J, Andrade MF, Zhang H, Ball M, Stanimirovic DB. The expression and functional characterization of ABCG2 in brain endothelial cells and vessels. FASEB J. 2003 Nov;17(14):2085-7. Epub 2003 Sep 4. PMID:12958161 doi:http://dx.doi.org/10.1096/fj.02-1131fje
↑ Desuzinges-Mandon E, Arnaud O, Martinez L, Huche F, Di Pietro A, Falson P. ABCG2 transports and transfers heme to albumin through its large extracellular loop. J Biol Chem. 2010 Oct 22;285(43):33123-33. doi: 10.1074/jbc.M110.139170. Epub, 2010 Aug 12. PMID:20705604 doi:http://dx.doi.org/10.1074/jbc.M110.139170
↑ Nakayama A, Matsuo H, Takada T, Ichida K, Nakamura T, Ikebuchi Y, Ito K, Hosoya T, Kanai Y, Suzuki H, Shinomiya N. ABCG2 is a high-capacity urate transporter and its genetic impairment increases serum uric acid levels in humans. Nucleosides Nucleotides Nucleic Acids. 2011 Dec;30(12):1091-7. doi:, 10.1080/15257770.2011.633953. PMID:22132962 doi:http://dx.doi.org/10.1080/15257770.2011.633953
↑ Kobuchi H, Moriya K, Ogino T, Fujita H, Inoue K, Shuin T, Yasuda T, Utsumi K, Utsumi T. Mitochondrial localization of ABC transporter ABCG2 and its function in 5-aminolevulinic acid-mediated protoporphyrin IX accumulation. PLoS One. 2012;7(11):e50082. doi: 10.1371/journal.pone.0050082. Epub 2012 Nov 26. PMID:23189181 doi:http://dx.doi.org/10.1371/journal.pone.0050082

1 Structural highlights
2 Function
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6hzm"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6hzm is ON HOLD  until Paper Publication
+==Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)==
+<StructureSection load='6hzm' size='340' side='right' caption='[[6hzm]], [[Resolution|resolution]] 3.09&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6hzm]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HZM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HZM FirstGlance]. <br>
-Description:
+</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>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6hbu|6hbu]]</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=6hzm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hzm OCA], [http://pdbe.org/6hzm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hzm RCSB], [http://www.ebi.ac.uk/pdbsum/6hzm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hzm ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/ABCG2_HUMAN ABCG2_HUMAN]] High-capacity urate exporter functioning in both renal and extrarenal urate excretion. Plays a role in porphyrin homeostasis as it is able to mediates the export of protoporhyrin IX (PPIX) both from mitochondria to cytosol and from cytosol to extracellular space, and cellular export of hemin, and heme. Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a major role in the multidrug resistance phenotype of several cancer cell lines. Implicated in the efflux of numerous drugs and xenobiotics: mitoxantrone, the photosensitizer pheophorbide, camptothecin, methotrexate, azidothymidine (AZT), and the anthracyclines daunorubicin and doxorubicin.<ref>PMID:12958161</ref> <ref>PMID:20705604</ref> <ref>PMID:22132962</ref> <ref>PMID:23189181</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Jackson, S M]]
+[[Category: Kowal, J]]
+[[Category: Locher, K P]]
+[[Category: Manolaridis, I]]
+[[Category: Stahlberg, H]]
+[[Category: Taylor, N M.I]]
+[[Category: Cancer]]
+[[Category: Membrane protein]]
+[[Category: Multidrug transporter]]

6hzm

From Proteopedia

Revision as of 08:21, 14 November 2018

Cryo-EM structure of the ABCG2 E211Q mutant bound to ATP and Magnesium (alternative placement of Magnesium into the cryo-EM density)

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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