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

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Cited 0 time in scopus
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dc.contributor.authorLee, Chang Woo-
dc.contributor.authorLee, Jun Hyuck-
dc.contributor.authorKim, Il-Chan-
dc.contributor.authorPark, Hyun-
dc.contributor.authorYim, Joung Han-
dc.contributor.authorJeong Ho Chang-
dc.contributor.authorHyun Ho Park-
dc.contributor.authorLee, Sung Gu-
dc.contributor.authorRyeo-Ok Kim-
dc.contributor.authorHackwon Do-
dc.contributor.authorKim, Jung Eun-
dc.date.accessioned2018-03-29T06:05:51Z-
dc.date.available2018-03-29T06:05:51Z-
dc.date.issued2015-
dc.identifier.urihttps://repository.kopri.re.kr/handle/201206/7355-
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 A, 2.2 A, and 2.3 A, respectively. The pFABP4 and pFABP5 proteins have a canonical β-barrel structure with two short α-helices that form a cap region and fatty acid ligand binding sites in the hydrophobic cavity within the β-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 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 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.-
dc.languageEnglish-
dc.titleStructural basis for the ligand-binding specificity of fatty acid-binding proteins (pFABP4 and pFABP5) in gentoo penguin-
dc.title.alternative젠투펭귄 유래 지방산 결합단백질의 구조 연구-
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(1): 12-18.-
dc.citation.titleBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS-
dc.citation.volume465-
dc.citation.number1-
dc.identifier.doi10.1016/j.bbrc.2015.07.087-
dc.citation.startPage12-
dc.citation.endPage18-
dc.description.articleClassificationSCI-
dc.description.jcrRateJCR 2013:65.63573883161511-
dc.subject.keywordFatty acid-binding protein-
dc.subject.keywordGentoo penguin (Pygoscelis papua)-
dc.subject.keywordX-ray crystallography-
dc.subject.keywordcrystal structure-
dc.subject.keywordβ-barrel protein-
dc.identifier.localId2015-0095-
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
2011-2016, Exploration of Future Resources in The Polar Oceans and Study on Their Utilization (K-POD) (11-16) / Yim; Joung Han
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