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Figure 1
Overview of FABP isoform structures. The overall β-barrel fold of the hFABP4 structure PDB entry 7g0n is shown at the top left with the chain colored in a rainbow from the N-terminus to the C-terminus (marked). No ligand is bound in this structure, which was generated from delipidated hFABP4. The helical lid and β-hairpin latch are indicated by spheres. All structures in gray are side-by-side arrangements of the FABP isoforms discussed here in their apo or native fatty acid-bound states (blue stick model). The palmitate from PDB entry 2hnx is shown as a reference (black). Three fatty acid-interacting residues, Arg107, Arg127 and Tyr129 (hFABP4 numbering), are shown as stick models. They are conserved except for in hFABP1, which has threonine and serine at the positions of the two arginine residues.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
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