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![[Figure 8]](gm5114fig8mag.jpg)
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Figure 8
Inhibitor binding and its effect on lid and latch gating residues. All ligand-bound structures of hFABP4 (top) and hFABP5 (bottom) were superimposed and the conformations of the side chains of the gating residues were analyzed. In hFABP4 the gating residue Phe58 on the latch appears to be flexible, while the opposing gating residue Val33 on the lid retains its rotamer. In hFABP5 the situation is reversed, with the gating residue Leu60 on the latch appearing to be static and the gating residue Met35 on the lid being flexible. The side chains of Phe17, Arg127 and Tyr129 are shown as green stick models for reference. The three-dimensional nonclassical NLS, Lys24, Arg33 and Lys34 in hFABP, is indicated by green spheres. |
![[Figure 8]](gm5114fig8.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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