 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 5]](mh5108fig5mag.jpg)
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Figure 5
Conserved features in FABP sequences and structures. (a) Sequence alignment of the human FABP family. Secondary-structure elements of P2 are shown at the top and the following features are highlighted at the bottom: Pro38 (black triangle), fatty acid-coordinating polar residues (blue triangles), main hydrophobic membrane contacts (green asterisks), main hydrophilic contacts (red asterisks) and other hydrophilic contacts (orange asterisks). See Fig. 8 ![[link]](../../../../../../logos/arrows/d_arr.gif) (b) and Supplementary Fig. S1 for details of the contacts obtained using MD. (b) The geometry at the anion-binding site in FABPs with a collisional mechanism and a conserved Pro38. (c) The same site in FABPs without Pro38. The dashed lines indicate coordination of the bound citrate in the P2 structure. The following PDB entries were superimposed on the human P2 structure: 3vg7
(FABP1; Sharma et al., 2012), 1ifc
(FABP2; Scapin et al., 1992), 1hmr
(FABP3; Young et al., 1994), 3p6d
(FABP4; J. M. Gonzalez & E. Pozharski, unpublished work), 1b56
(FABP5; Hohoff et al., 1999), 3elx
(FABP6; Capaldi et al., 2009), 1fdq
(FABP7; Balendiran et al., 2000), 4a60
(FABP9; J. R. C. Muniz, W. Kiyani, L. Shrestha, D. S. Froese, T. Krojer, M. Vollmar, C. H. Arrowsmith, A. M. Edwards, J. Weigelt, C. Bountra, F. Von Delft & W. W. Yue, unpublished work), 1crb
(CRBP1; Cowan et al., 1993) and 2rct
(CRBP2; Tarter et al., 2008). |
![[Figure 5]](mh5108fig5.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
