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タイトル: Identification of Functionally Important Residues of the Silkmoth Pheromone Biosynthesis-activating Neuropeptide Receptor, an Insect Ortholog of the Vertebrate Neuromedin U Receptor
著者: Kawai, Takeshi
Katayama, Yukie
Guo, Linjun
Liu, Desheng
Suzuki, Tatsuya
Hayakawa, Kou
Lee, Jae Min
Nagamine, Toshihiro
Hull, J. Joe
Matsumoto, Shogo
Nagasawa, Hiromichi
Tanokura, Masaru
Nagata, Koji
著者(別言語): 河合, 岳志
片山, 幸江
郭, 琳珺
刘, 德生
鈴木, 達也
早川, 江
李, 載旼
永峰, 俊弘
松本, 正吾
長澤, 寛道
田之倉, 優
永田, 宏次
キーワード: G-protein-coupled Receptor (GPCR)
Molecular Docking
Molecular Modeling
Peptide Hormone
Receptor Structure-Function
Silkworm
FXPRX-amide Motif
Ligand-Receptor Interaction
Neuromedin U
Sex Pheromone Biosynthesis
発行日: 2014年7月4日
出版者: The American Society for Biochemistry and Molecular Biology
掲載誌情報: The Journal of Biological Chemistry. 2014, 289:19150-19163. doi: 10.1074/jbc.M113.488999
関連URI: http://www.u-tokyo.ac.jp/ja/utokyo-research/research-news/similarities-in-moth-pheromone-synthesis-and-human-stress-appetite-control/
http://www.u-tokyo.ac.jp/en/utokyo-research/research-news/similarities-in-moth-pheromone-synthesis-and-human-stress-appetite-control/
http://www.jbc.org/content/289/27/19150.abstract
抄録: The biosynthesis of sex pheromone components in many lepidopteran insects is regulated by the interaction between pheromone biosynthesis-activating neuropeptide (PBAN) and the PBAN receptor (PBANR), a class A G-protein-coupled receptor. To identify functionally important amino acid residues in the silkmoth PBANR, a series of 27 alanine substitutions was generated using a PBANR chimera C-terminally fused with enhanced GFP. The PBANR mutants were expressed in Sf9 insect cells, and their ability to bind and be activated by a core PBAN fragment (C10PBANR2K) was monitored. Among the 27 mutants, 23 localized to the cell surface of transfected Sf9 cells, whereas the other four remained intracellular. Reduced binding relative to wild type was observed with 17 mutants, and decreased Ca2+ mobilization responses were observed with 12 mutants. Ala substitution of Glu-95, Glu-120, Asn-124, Val-195, Phe-276, Trp-280, Phe-283, Arg-287, Tyr-307, Thr-311, and Phe-319 affected both binding and Ca2+ mobilization. The most pronounced effects were observed with the E120A mutation. A molecular model of PBANR indicated that the functionally important PBANR residues map to the 2nd, 3rd, 6th, and 7th transmembrane helices, implying that the same general region of class A G-protein-coupled receptors recognizes both peptidic and nonpeptidic ligands. Docking simulations suggest similar ligand-receptor recognition interactions for PBAN-PBANR and the orthologous vertebrate pair, neuromedin U (NMU) and NMU receptor (NMUR). The simulations highlight the importance of two glutamate residues, Glu-95 and Glu-120, in silkmoth PBANR and Glu-117 and Glu-142 in human NMUR1, in the recognition of the most functionally critical region of the ligands, the C-terminal residue and amide.
内容記述: UTokyo Research掲載「蛾の性フェロモン生合成と人のストレス・食欲制御の類似性」 URI: http://www.u-tokyo.ac.jp/ja/utokyo-research/research-news/similarities-in-moth-pheromone-synthesis-and-human-stress-appetite-control/
UTokyo Research: "Similarities in moth pheromone synthesis and human stress/appetite control" URI: http://www.u-tokyo.ac.jp/en/utokyo-research/research-news/similarities-in-moth-pheromone-synthesis-and-human-stress-appetite-control/
URI: http://hdl.handle.net/2261/57057
ISSN: 0021-9258 (print)
1083-351X (online)
出現カテゴリ:014 自然科学
1160410 学術雑誌論文

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