Structure−Function Relationships of Multidrug Resistance P-Glycoprotein


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PAJEVA, Ilza K., Christoph GLOBISCH, Michael WIESE, 2004. Structure−Function Relationships of Multidrug Resistance P-Glycoprotein. In: Journal of Medicinal Chemistry. 47(10), pp. 2523-2533. ISSN 0022-2623. eISSN 1520-4804. Available under: doi: 10.1021/jm031009p

@article{Pajeva2004-05Struc-38061, title={Structure−Function Relationships of Multidrug Resistance P-Glycoprotein}, year={2004}, doi={10.1021/jm031009p}, number={10}, volume={47}, issn={0022-2623}, journal={Journal of Medicinal Chemistry}, pages={2523--2533}, author={Pajeva, Ilza K. and Globisch, Christoph and Wiese, Michael} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:creator>Pajeva, Ilza K.</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:language>eng</dc:language> <dspace:isPartOfCollection rdf:resource=""/> <dcterms:isPartOf rdf:resource=""/> <dcterms:available rdf:datatype="">2017-03-17T10:35:46Z</dcterms:available> <dc:contributor>Pajeva, Ilza K.</dc:contributor> <dcterms:abstract xml:lang="eng">The direct structure-function relationships of P-glycoprotein (P-gp) are presently unknown. In this paper two P-gp models are described: a homology model based on the Escherichia coli MsbA lipid transporter and a model based on the cross-linking results of Loo and Clarke. The pharmacophore pattern for the H-site (Hoechst 33342) is derived and binding sites on the transmembrane domains TM5 and TM11 are identified. Binding sites of rhodamines are also proposed on TM6 and TM12 in accordance with the published data. Location of the binding sites is opposite in both models, suggesting that TMs undergo rotation exposing the substrate bound from the membrane to the pore. It has been concluded that the models derived represent two different functional states of P-gp corresponding to nucleotide-free and nucleotide-bound P-gp. A qualitative correspondence to the P-gp crystallographic structure at 20 A resolution is found. A hypothesis is proposed about rearrangement of TMs upon state transition.</dcterms:abstract> <dcterms:issued>2004-05</dcterms:issued> <bibo:uri rdf:resource=""/> <dc:date rdf:datatype="">2017-03-17T10:35:46Z</dc:date> <dc:creator>Wiese, Michael</dc:creator> <dcterms:title>Structure−Function Relationships of Multidrug Resistance P-Glycoprotein</dcterms:title> <dc:contributor>Globisch, Christoph</dc:contributor> <dc:creator>Globisch, Christoph</dc:creator> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dc:contributor>Wiese, Michael</dc:contributor> </rdf:Description> </rdf:RDF>

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