Title : Cholesterol Asymmetrically Modulates the Conformational Ensemble of the Nucleotide-Binding Domains of P-Glycoprotein in Lipid Nanodiscs.

Pub. Date : 2021 Jan 12

PMID : 33350827






3 Functional Relationships(s)
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1 Cholesterol Asymmetrically Modulates the Conformational Ensemble of the Nucleotide-Binding Domains of P-Glycoprotein in Lipid Nanodiscs. Cholesterol ATP binding cassette subfamily B member 1 Homo sapiens
2 We aimed to determine the effects of cholesterol in a membrane on the conformational behavior of P-gp in lipid nanodiscs. Cholesterol ATP binding cassette subfamily B member 1 Homo sapiens
3 Hydrogen/deuterium exchange mass spectrometry demonstrates that cholesterol in the membrane induces asymmetric, long-range changes in the distributions and exchange kinetics of conformations of the nucleotide-binding domains, correlating the effects of lipid composition on activity with specific changes in the P-gp conformational landscape. Cholesterol ATP binding cassette subfamily B member 1 Homo sapiens