Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity.

Loo, Tip W

Cysteines introduced into extracellular loops 1 and 4 of human P-glycoprotein that are close only in the open conformation spontaneously form a disulfide bond that inhibits drug efflux and ATPase activity. [electronic resource] - The Journal of biological chemistry Sep 2014 - 24749-58 p. digital

Publication Type: Journal Article; Research Support, Non-U.S. Gov't

1083-351X

10.1074/jbc.M114.583021 doi


ATP Binding Cassette Transporter, Subfamily B--chemistry
Adenosine Triphosphatases--metabolism
Adenosine Triphosphate--metabolism
Animals
Binding Sites--genetics
Cell Line
Cysteine--chemistry
Disulfides--chemistry
Dithiothreitol--pharmacology
Drug Resistance, Multiple--drug effects
Glycoside Hydrolases--metabolism
HEK293 Cells
Humans
Hydrolysis
Immunoblotting
Models, Molecular
Mutation
Pharmaceutical Preparations--metabolism
Protein Conformation
Protein Structure, Secondary
Protein Structure, Tertiary