Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin
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- Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin
- Lee, Chang Woo
Kim, Jung Eun
Lee, Sung Gu
Park, Hyun Ho
Chang, Jeong Ho
Yim, Joung Han
Lee, Jun Hyuck
- Biochemistry & Molecular Biology; Biophysics
- Fatty acid-binding protein; β-barrel protein; Crystal structure; Gentoo penguin(Pygoscelis papua); X-ray crystallography
- Issue Date
- Lee, Chang Woo, et al. 2015. "Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin". Biochemical and Biophysical Research Communications,, 465: 12-18.
- Fatty acid-binding proteins (FABPs) are involved in transporting hydrophobic fatty acids between various aqueous compartments of the cell by directly binding ligands inside their β-barrel cavities. Here, we report the crystal structures of ligand-unbound pFABP4, linoleate-bound pFABP4, and palmitate-bound pFABP5, obtained from gentoo penguin (Pygoscelis papua), at a resolution of 2.1？, 2.2？, and 2.3？,respectively. The pFABP4 and pFABP5 proteins have a canonical b-barrel structure with two short ahelices that form a cap region and fatty acid ligand binding sites in the hydrophobic cavity within the bbarrel structure. Linoleate-bound pFABP4 and palmitate-bound pFABP5 possess different ligand-binding modes and a unique ligand-binding pocket due to several sequence dissimilarities (A76/L78, T30/M32, underlining indicates pFABP4 residues) between the two proteins. Structural comparison revealed significantly different conformational changes in the β3-β4 loop region (residues 57-62) as well as the flipped Phe60 residue of pFABP5 than that in pFABP4 (the corresponding residue is Phe58). A ligandbinding study using fluorophore displacement assays shows that pFABP4 has a relatively strong affinity for linoleate as compared to pFABP5. In contrast, pFABP5 exhibits higher affinity for palmitate than that for pFABP4. In conclusion, our high-resolution structures and ligand-binding studies provide useful insights into the ligand-binding preferences of pFABPs based on key proteineligand interactions.
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