1H, 15N and 13C resonance assignments of light organ-associated fatty acid-binding protein of Taiwanese fireflies

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• 作者：Kai-Li Tseng ; Yi-Zong Lee ; Yun-Ru Chen ; Ping-Chiang Lyu
• 关键词：Luciola cerata ; Light organ ; lcFABP ; Chemical shift assignments
• 刊名：Biomolecular NMR Assignments
• 出版年：2016
• 出版时间：April 2016
• 年：2016
• 卷：10
• 期：1
• 页码：71-74
• 全文大小：536 KB
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• 作者单位：Kai-Li Tseng (1)
  Yi-Zong Lee (1)
  Yun-Ru Chen (1)
  Ping-Chiang Lyu (1) (2)
  
  1. Institute of Bioinformatics and Structural Biology, National Tsing Hua University, No. 101, Sec. 2, Kuang Fu Rd, Hsinchu, 30013, Taiwan, ROC
  2. Department of Medical Sciences, National Tsing Hua University, Hsinchu, Taiwan, ROC
  
• 刊物类别：Physics and Astronomy
• 刊物主题：None Assigned
• 出版者：Springer Netherlands
• ISSN：1874-270X

文摘

Fatty acid-binding proteins (FABPs) are a family of proteins that modulate the transfer of various fatty acids in the cytosol and constitute a significant portion in many energy-consuming cells. The ligand binding properties and specific functions of a particular type of FABP seem to be diverse and depend on the respective binding cavity as well as the cell type from which this protein is derived. Previously, a novel FABP (lcFABP; lc: Luciola cerata) was identified in the light organ of Taiwanese fireflies. The lcFABP was proved to possess fatty acids binding capabilities, especially for fatty acids of length C₁₄–C₁₈. However, the structural details are unknown, and the structure–function relationship has remained to be further investigated. In this study, we finished the 1H, 15N and 13C chemical shift assignments of 15N/13C-enriched lcFABP by solution NMR spectroscopy. In addition, the secondary structure distribution was revealed based on the backbone N, H, C_α, H_α, C and side chain C_β assignments. These results can provide the basis for further structural exploration of lcFABP.