Background: The P-gp drug-binding domain is linked to the two nucleotide-binding domains (NBDs) by NBD1 and NBD2 transmission interfaces. Results: Only mutations at the NBD2 transmission interface blocked P-gp assembly. Tariquidar repaired all 25 mutants. Conclusion: The mechanism of P-gp folding requires precise hydrophobic interactions at the NBD2 interface. Significance: We identified a linchpin for assembly and repair of ABC proteins.
CITATION STYLE
Loo, T. W., & Clarke, D. M. (2015). The transmission interfaces contribute asymmetrically to the assembly and activity of human P-glycoprotein. Journal of Biological Chemistry, 290(27), 16954–16963. https://doi.org/10.1074/jbc.M115.652602
Mendeley helps you to discover research relevant for your work.