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

Cited 7 time in wos
Cited 7 time in scopus

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dc.contributor.authorLee, Chang Woo-
dc.contributor.authorKim, Jung Eun-
dc.contributor.authorDo, Hackwon-
dc.contributor.authorKim, Ryeo-Ok-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorPark, Hyun Ho-
dc.contributor.authorChang, Jeong Ho-
dc.contributor.authorYim, Joung Han-
dc.contributor.authorPark, Hyun-
dc.contributor.authorKim, Il-Chan-
dc.contributor.authorLee, Jun Hyuck-
dc.date.accessioned2017-08-03T13:40:09Z-
dc.date.available2017-08-03T13:40:09Z-
dc.date.issued2015-
dc.description.abstractFatty 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.-
dc.languageEnglish-
dc.subjectBiochemistry & Molecular Biology-
dc.subjectBiophysics-
dc.titleStructural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin-
dc.typeArticle-
dc.identifier.bibliographicCitationLee, Chang Woo, et al. 2015. "Structural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin". <em>Biochemical and Biophysical Research Communications,</em>, 465: 12-18.-
dc.citation.titleBiochemical and Biophysical Research Communications,-
dc.citation.volume465-
dc.citation.page12-18.-
dc.identifier.doi10.1016/j.bbrc.2015.07.087-
dc.subject.keywordFatty acid-binding protein-
dc.subject.keywordβ-barrel protein-
dc.subject.keywordCrystal structure-
dc.subject.keywordGentoo penguin(Pygoscelis papua)-
dc.subject.keywordX-ray crystallography-
dc.identifier.scopusid2-s2.0-84940438440-
dc.identifier.wosid000361417300004-
Appears in Collections  
2014-2016, Antarctic Organisms: Cold-Adaptation Mechanism and Its Application (14-16) / Park; Hyun (PE14070; PE15070; PE16070)
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