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Default Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.

Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.

Related Articles Flavonoid binding to a multi-drug-resistance transporter protein: an STD-NMR study.

Anal Bioanal Chem. 2004 Aug;379(7-8):1045-9

Authors: Nissler L, Gebhardt R, Berger S

Flavonoids are well known to inhibit the function of the multi-drug-resistance (mdr) transporter by interacting with their ATP binding domains. The precise orientation of these molecules inside the ATP binding pocket is still unclear. We applied the saturation transfer difference (STD) NMR technique to investigate the binding of the flavonoid luteolin and its 7-O-beta-D-glycopyranoside to the recombinant nucleotide binding domain (NBD2) of mouse-mdr. First, this NMR technique confirmed binding of both ligands to NBD2, as was determined from tryptophan fluorescence-quenching experiments. Further, the results suggest binding of both luteolin and its 7-O-beta-D-glycopyranoside by their polar groups at positions 4, 5, and 3' to the protein.

PMID: 15241579 [PubMed - indexed for MEDLINE]



Source: PubMed
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