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• W4300863128 abstract "Intracellular transport of fatty acids involves binding of ligands to their carrier fatty acid binding proteins (FABPs) and interactions of ligand-free and -bound FABPs with membranes. Previous studies focused on ligand-free FABPs. Here, our amide hydrogen exchange data showed that oleic acid binding to human intestinal FABP (hIFABP) stabilizes the protein, most likely through enhancing the hydrogen-bonding network, and induces rearrangement of sidechains even far away from the ligand binding site. Using NMR relaxation techniques, we found that the ligand binding affects not only conformational exchanges between major and minor states but also the affinity of hIFABP to nanodiscs. Analyses of the relaxation and amide exchange data suggested that two minor native-like states existing in both ligand-free and -bound hIFABPs originate from global breathing motions, while one minor native-like state comes from local motions. The amide hydrogen exchange data also indicated that helix αII undergoes local unfolding through which ligands can exit from the binding cavity." @default.
• W4300863128 created "2022-10-04" @default.
• W4300863128 creator A5027928580 @default.
• W4300863128 creator A5042821318 @default.
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• W4300863128 date "2022-11-01" @default.
• W4300863128 modified "2023-09-27" @default.
• W4300863128 title "Effects of ligand binding on dynamics of fatty acid binding protein and interactions with membranes" @default.
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• W4300863128 doi "https://doi.org/10.1016/j.bpj.2022.09.043" @default.
• W4300863128 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/36196055" @default.
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