Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin

Title
Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin
Author(s)
박현호이창우[이창우]김정은[김정은]도학원[도학원]김려옥[김려옥]이상구[이상구]장정호[장정호]임정한[임정한]박현[박현]김일찬[김일찬]이준혁[이준혁]
Keywords
BACKBONE DYNAMICS; CRYSTAL-STRUCTURE; LIVER; FAMILY
Issue Date
201509
Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
Citation
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.465, no.1, pp.12 - 18
Abstract
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 beta-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 angstrom, 2.2 angstrom, and 2.3 angstrom, respectively. The pFABP4 and pFABP5 proteins have a canonical beta-barrel structure with two short alpha-helices that form a cap region and fatty acid ligand binding sites in the hydrophobic cavity within the beta-barrel 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 beta 3-beta 4 loop region (residues 57-62) as well as the flipped Phe60 residue of pFABP5 than that in pFABP4 (the corresponding residue is Phe58). A ligand-binding 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 protein-ligand interactions. (C) 2015 Elsevier Inc. All rights reserved.
URI
http://hdl.handle.net/YU.REPOSITORY/31100http://dx.doi.org/10.1016/j.bbrc.2015.07.087
ISSN
0006-291X
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이과대학 > 화학생화학부 > Articles
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