波谱学杂志 ›› 2012, Vol. 29 ›› Issue (1): 60-67.

• 研究论文 • 上一篇    下一篇

杆状病毒蛋白融合肽LdF在溶液中的NMR结构研究

熊景文1,2,曾丹云1,2,姜凌1*,刘买利1   

  1. 1. 波谱与原子分子物理国家重点实验室,武汉磁共振中心(中国科学院 武汉物理与数学研究所),湖北 武汉 430071; 
    2.中国科学院 研究生院,北京 100049
  • 收稿日期:2011-03-31 修回日期:2011-05-31 出版日期:2012-03-05 发布日期:2012-03-05
  • 基金资助:

    国家自然科学基金资助项目(90813017,20921004);武汉市晨光计划资助项目(200950431221).

NMR Analyses of Fusion Peptide of the Lymantria Dispar Multiple Nucleopolyhedrovirus F Protein

 XIONG Jing-Wen1,2, ZENG Dan-Yun1,2, JIANG Ling1*, LIU Mai-Li1   

  1. 1. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Center for Magnetic Resomance (Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences), Wuhan 430071,  China;
    2. Graduate School of the Chinese Academy of Sciences, Beijing 100049, China
  • Received:2011-03-31 Revised:2011-05-31 Online:2012-03-05 Published:2012-03-05
  • Supported by:

    国家自然科学基金资助项目(90813017,20921004);武汉市晨光计划资助项目(200950431221).

摘要:

LD130是舞毒蛾核多角体病毒(Lymantria dispar multiple nucleopolyhedrovirus, LdMNPV)的膜融合蛋白(F蛋白),其F1亚基N端疏水的保守区为介导膜融合过程的活性肽段,即融合肽区域. 利用核磁共振的方法,确定了该融合肽在酸性条件下类膜环境中的溶液结构. 结果表明融合肽LdF具有典型的α螺旋结构,整个肽段于类膜环境中呈现两亲性,即螺旋沿轴向可分为亲水侧面和亲脂侧面. 该结构有利于对病毒囊膜与细胞膜融合过程的深入理解与研究.

关键词: 核磁共振(NMR), 结构, 2D NMR, 杆状病毒融合肽

Abstract:

LD130 is the fusion protein of baculoviruse Lymantria dispar multiple nucleopolyhedrovirus (LdMNPV). The N terminal conserved region of subunit F1 in LD130 is the fusion peptide, which actively induces membrane fusion processes. NMR methods were used to identify the solution structure of the fusion peptide under membrane simulated enviornment at low pH. The fusion peptide appeared to be an amphiphilic structure composed of a flexible coil in the N-terminus, and a regular α-helix from L3 to V16. The structure of the LD130 fusion peptide allows us to further investigate the structure-functional relationship of the fusion peptide.

Key words: NMR, structure, 2D NMR, fusion peptide of baculoviruse

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