4m2s
From Proteopedia
(Difference between revisions)
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- | + | {{STRUCTURE_4m2s| PDB=4m2s | SCENE= }} | |
+ | ===Corrected Structure of Mouse P-glycoprotein bound to QZ59-RRR=== | ||
+ | {{ABSTRACT_PUBMED_24155053}} | ||
- | + | ==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> | ||
- | + | ==About this Structure== | |
+ | [[4m2s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4M2S OCA]. | ||
- | + | ==Reference== | |
+ | <ref group="xtra">PMID:024155053</ref><references group="xtra"/><references/> | ||
+ | [[Category: Mus musculus]] | ||
+ | [[Category: Xenobiotic-transporting ATPase]] | ||
+ | [[Category: Aller, S G.]] | ||
+ | [[Category: Jaimes, K F.]] | ||
+ | [[Category: Li, J.]] | ||
+ | [[Category: Adenosine triphosphate]] | ||
+ | [[Category: Atp-binding cassette transporter]] | ||
+ | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
+ | [[Category: Multidrug efflux]] |
Revision as of 08:16, 13 November 2013
Contents |
Corrected Structure of Mouse P-glycoprotein bound to QZ59-RRR
Template:ABSTRACT PUBMED 24155053
Function
[MDR1A_MOUSE] Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.[1]
About this Structure
4m2s is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
- Li J, Jaimes KF, Aller SG. Refined structures of mouse P-Glycoprotein. Protein Sci. 2013 Oct 24. doi: 10.1002/pro.2387. PMID:24155053 doi:http://dx.doi.org/10.1002/pro.2387
- ↑ Aller SG, Yu J, Ward A, Weng Y, Chittaboina S, Zhuo R, Harrell PM, Trinh YT, Zhang Q, Urbatsch IL, Chang G. Structure of P-glycoprotein reveals a molecular basis for poly-specific drug binding. Science. 2009 Mar 27;323(5922):1718-22. PMID:19325113 doi:323/5922/1718