波谱学杂志 ›› 2011, Vol. 28 ›› Issue (2): 290-298.

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A3G蛋白结构与功能NMR研究的最新进展

代媛媛1,2,蓝文贤2*,常城1*   

  1. 1. 兰州大学 生命科学学院,甘肃 兰州 730000; 
    2. 中国科学院 上海有机化学研究所,生命有机化学国家重点实验室,上海 200032
  • 收稿日期:2010-06-18 修回日期:2010-07-12 出版日期:2011-06-05 发布日期:2011-06-05
  • 基金资助:

    国家重点基础研究发展计划资助项目(2009CB918601);国家自然科学青年基金资助项目(20905074).

Progress in NMRBased Studies on the Structure and Function of A3G

 DAI Yuan-Yuan1,2, LA Wen-Xian2*, CHANG Cheng1*   

  1. 1. School of Life Sciences, Lanzhou University, Lanzhou 730000, China;
    2. State Key Lab of BioOrganic and Natural Products Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai 200032, China
  • Received:2010-06-18 Revised:2010-07-12 Online:2011-06-05 Published:2011-06-05
  • Supported by:

    国家重点基础研究发展计划资助项目(2009CB918601);国家自然科学青年基金资助项目(20905074).

摘要:

A3G(apolipoprotin B mRNA-editing catalytic polypeptide 3 protein G)是一种天然抗病毒活性的胞嘧啶脱氨基酶,具有广谱的抗病毒作用,属于人体固有的免疫蛋白分子. 在HIV病毒复制过程中,A3G蛋白能进入新生成的病毒颗粒内部,诱导病毒cDNA胞嘧啶脱氨基化变为尿嘧啶,阻断病毒复制,从而导致病毒活性丧失. 最近几年,许多实验室以NMR技术和X射线衍射技术为基础,开展了一系列A3G蛋白的结构生物学和脱氨基化反应动态过程的研究,取得了具有重要意义的研究进展,为后期的研究工作提供了很好的新思路. 通过对这些工作进行总结,以期为我国艾滋病、乙肝病毒的防治,及相关药物分子的设计提供新的借鉴.

关键词: A3G,  HIV, NMR, X射线衍射

Abstract:

The human A3G (apolipoprotein B messenger-RNA editing enzyme, catalytic polypeptide-like 3G) protein belongs to a family of polynucleotide cytidine deaminases, which is a human intrinsic immune protein with anti-viral activity. During the process of HIV virions replication, A3G is effectively incorporated into budding HIV-1 virions, catalyze C→U conversions, and then block viral replication, resulting in viral infectivity. In recent years, much attention has been paid on the structure and the process of deamination of A3G by NMR or X-ray, and significant research progress has been made, which might provide new ideal for further research. In this paper, we summarized these works in order to provide new reference for the prevention and treatment of AID’s and hepatitis B virus and the relative new drug design.

Key words: A3G, HIV, NMR, X-ray diffraction

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