The transmembrane domains of the human multidrug resistance P-glycoprotein are sufficient to mediate drug binding and trafficking to the cell surface.

Abstract excerpt

The human multidrug resistance P-glycoprotein (P-gp) is organized in two tandem repeats with each repeat consisting of an N-terminal hydrophobic domain containing six potential transmembrane segments followed by a hydrophilic domain containing a nucleotide-binding fold. A series of deletion mutants together with an in vivo drug-binding assay were used to test whether the deletion mutants interacted with...

Topics

• ATP Binding Cassette Transporter, Subfamily B, Member 1
• Binding Sites
• Capsaicin
• Cell Line
• Cyclosporine
• Gene Expression Regulation
• Glycosylation
• Hexosaminidases
• Humans
• Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
• Membrane Proteins
• Mutation
• Nucleotides
• Peptide Fragments