Structure and sequence analysis of influenza A virus nucleoprotein

作     者：NG Andy Ka-Leung SHAW Pang-Chui 

作者机构：Molecular Biotechnology Programme Department of Biochemistry and Centre for Protein Science and Crystallography The Chi-nese University of Hong Kong 

出 版 物：《Science China(Life Sciences)》 (中国科学（生命科学英文版）)

年 卷 期：2009年第52卷第5期

页      面：439-449页

核心收录：

学科分类：0710[理学-生物学] 0830[工学-环境科学与工程（可授工学、理学、农学学位）] 1001[医学-基础医学(可授医学、理学学位)] 100103[医学-病原生物学] 10[医学] 

基　　金：supported by a General Research Fund (CUHK472808) from the Research Grants Council of Hong Kong SAR. J.H. Wang’s group was supported by the Claudia Adams Barr Program in Cancer Research. 

主　　题：Influenza H5N1 nucleoprotein oligomerization RNA binding 

摘      要：Influenza A virus nucleoprotein (NP) forms homo-oligomers and multiple copies of NP wrap around genomic RNA, along with a trimeric polymerase making up ribonucleoprotein (RNP) complex. Sequence comparison of more than 2500 influenza A NP showed that this protein contains 30.1 % of polymorphic residues. NP is composed of a head and a body domain and a tail loop/ linker region. The head domain is more conserved than the body domain, as revealed from the structure-based sequence alignment. NP oligomerization is mediated by the insertion of the non-polymorphic and structurally conserved tail loop of one NP molecule to a groove of another NP. The different form of NP oligomers is due to the flexibility of the polymorphic linkers that join the tail loop to the rest of the protein. The RNA binding property of NP is known to involve the protruding element and the flexible basic loop between the head and body domains, both having high degree of primary sequence conservation. To bind RNA, NP may first capture the RNA by the flexible basic loop and then the RNA is clamped by the protruding element.