A high-resolution data set of fatty acid-binding protein structures. I. Dynamics of FABP4 and ligand binding

Casagrande, F.; Ehler, A.; Burger, D.; Benz, J.; Ross, A.; Rudolph, M.G.

doi:10.1107/S2059798325006242

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 6
Chemical shift perturbations of hFABP4 upon fatty acid (a) and inhibitor (b) binding to apo hFABP4. The tetrazole and cyclopentenyl carboxylate (thiophene) inhibitors have IC₅₀ values of 50 nM and 23 nM, respectively. Different fatty acids and inhibitors induce specific conformations in hFABP4. The right-hand panels show overlays to highlight the different conformations induced by the three fatty acids (a) and the two inhibitors (b).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 81| Part 8| August 2025| Pages 423-435

https://doi.org/10.1107/S2059798325006242

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