Title : Molecular model of the outward facing state of the human P-glycoprotein (ABCB1), and comparison to a model of the human MRP5 (ABCC5).

Pub. Date : 2007 Sep 6

PMID : 17803828






3 Functional Relationships(s)
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1 RESULTS: In order to elucidate structural and molecular concepts of multidrug resistance, we have constructed a molecular model of the ATP-bound outward facing conformation of the human multidrug resistance protein ABCB1 using the Sav1866 crystal structure as a template, and compared the ABCB1 model with a previous ABCC5 model. Adenosine Triphosphate ATP binding cassette subfamily C member 5 Homo sapiens
2 In contrast, EPS of the ABCC5 substrate translocation chamber, which transports organic anions, was generally positive. eps ATP binding cassette subfamily C member 5 Homo sapiens
3 The EPS in the substrate translocation chambers and the positive-negative ratio of charged amino acids were in accordance with the transport of cationic amphiphilic and lipophilic substrates by ABCB1, and the transport of organic anions by ABCC5. eps ATP binding cassette subfamily C member 5 Homo sapiens