Chinese Journal of Magnetic Resonance ›› 2011, Vol. 28 ›› Issue (2): 290-298.

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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).

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

CLC Number: