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Lysine 268 adjacent to transmembrane helix 5 of hamster P‐glycoprotein is the major photobinding site of iodomycin in CHO B30 cells
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Lysine 268 adjacent to transmembrane helix 5 of hamster P‐glycoprotein is the major photobinding site of iodomycin in CHO B30 cells
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Lysine 268 adjacent to transmembrane helix 5 of hamster P‐glycoprotein is the major photobinding site of iodomycin in CHO B30 cells
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Journal Article
Lysine 268 adjacent to transmembrane helix 5 of hamster P‐glycoprotein is the major photobinding site of iodomycin in CHO B30 cells
2021
Overview
P‐glycoprotein (Pgp) detoxifies cells by exporting hundreds of chemically dissimilar hydrophobic and amphipathic compounds and is implicated in multidrug resistance (MDR) in the treatment of cancers. Photoaffinity labeling of plasma membrane vesicles of MDR CHO B30 cells with the anthracycline [125I]‐iodomycin, subsequent sequential cleavage with BNPS‐skatol and endoproteinase Lys‐C, and the Edman sequencing of the purified photoaffinity‐labeled peptide identified the lysine residue at position 268 in the hamster Pgp primary sequence as the major photobinding site of iodomycin in CHO B30 cells. Lysine 268 is located adjacent to the cytosolic terminus of transmembrane 5. According to thermodynamic and kinetic analyses, this location should present the equilibrium binding site of ATP‐free Pgp for daunomycin and iodomycin in B30 cells. The multidrug transporter P‐glycoprotein (Pgp) exports hundreds of chemically dissimilar compounds. Whilst crystallography and cryo‐electron microscopy localized drug binding sites of reconstituted recombinant Pgp in the centre or the ectoplasmic site of the bilayer, we identified the binding site for the anthracycline iodomycin in native plasma membranes at the border between the transmembrane domains and the nucleotide binding sites of Pgp.
Publisher
John Wiley & Sons, Inc,John Wiley and Sons Inc,Wiley
Subject
/ Animals
/ ATP Binding Cassette Transporter, Subfamily B, Member 1 - chemistry
/ ATP Binding Cassette Transporter, Subfamily B, Member 1 - metabolism
/ Daunorubicin - analogs & derivatives
/ hamsters
/ Humans
/ Iodine Radioisotopes - chemistry
/ Iodine Radioisotopes - metabolism
/ Labeling
/ Lysine
/ Membrane Glycoproteins - chemistry
/ Membrane Glycoproteins - pharmacology
/ Ovaries
/ Peptides
/ Plasma
/ Protein Interaction Domains and Motifs
/ Proteins
/ Solvents
