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

Figure 3
Fatty acid-binding conformations in FABPs. The orientation is the same as in Fig. 1

. Fatty acids are colored according to their labels. (a) Comparison of different human FABP isoforms. Purified, delipidated, refolded and crystallized hFABP4 yields an apo form (magenta water molecules). Palmitate (pal) bound to hFABP4 (PDB entry 2hnx; black) forms a U shape as does myristate (myr; shades of blue) in the other isoforms, with the exception of myristate bound to hFABP9, where the fatty acid adopts the L conformation (PDB entry 7fyl; light blue). Key interacting residues are shown with numbering following that of hFABP4 and arrows point to the locations of possible hydrogen bonds between carboxylates and FABP side chains. (b) Comparison of U- and L-shaped conformations in human and mouse FABP4 bound to longer and unsaturated fatty acids. pal-hFABP4 is again shown as a reference (black). Linoleic acid (lin; yellow) has two cis double bonds and forms a tight turn. Arachidonic acid (ara; red) has four cis double bonds and adopts a wider U shape than linoleic acid. Oleic acid (ola; blue) with a single cis double bond, as well as the saturated long stearic acid (ste; gray), adopt the L shape, and their alkyl chains extend into bulk solvent. Of note, the shorter saturated palmitic acid adopts the L shape in mouse FABP4 (green) but an U shape in human FABP4 (black).

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798325006242

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