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![[Figure 10]](gm5115fig10mag.jpg)
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Figure 10
Membrane-interacting residues in hFABP4. (a) HSQC spectra of hFABP4 were recorded in the absence (black) and presence (red) of a DMPG:DHCP mixed micelle of q = 0.1. Comparison of the spectra shows chemical shifts δ even at this small q-value. (b) The plot of δ as a function of sequence position shows the lid and latch regions to exhibit the largest chemical shifts, indicating binding of these regions to the mixed micelle. (c) Model of FABP4 binding to a membrane (based on Bolterauer & Heller, 1996  ) via its lid and latch regions. The magnitude of the chemical shifts is shown as the thickness of the green tube. (d) The asymmetric charge distribution in hFABP4 supports this membrane-interaction model. The electrostatic potential of PDB entry 8s1k was calculated with APBS (Jurrus et al., 2018) and displayed as ±2kBT/e. The portal region (lid and latch) and the entry portal are highlighted along with the latch residue Phe58 and the nonclassical NLS Lys21, Arg30 and Lys31. The portal region is positively charged (blue) with a ring of negative potential (red) below it. |
![[Figure 10]](gm5115fig10.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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