Crystal Structure of the Nipah Virus Phosphoprotein Tetramerization Domain

被引：72
作者：
Bruhn, Jessica F. [1 ]
Barnett, Katherine C. [1 ]
Bibby, Jaclyn [2 ]
Thomas, Jens M. H. [3 ]
Keegan, Ronan M. [4 ]
Rigden, Daniel J. [3 ]
Bornholdt, Zachary A. [1 ]
Saphire, Erica Ollmann [1 ,5 ]
机构：
[1] Scripps Res Inst, Dept Immunol & Microbial Sci, La Jolla, CA 92037 USA
[2] Univ Liverpool, Robert Robinson Labs, Dept Chem, Liverpool L69 3BX, Merseyside, England
[3] Univ Liverpool, Inst Integrat Biol, Liverpool L69 3BX, Merseyside, England
[4] STFC Rutherford Appleton Lab, RCaH, Chilton, England
[5] Scripps Res Inst, Skaggs Inst Chem Biol, La Jolla, CA 92037 USA
来源：
JOURNAL OF VIROLOGY | 2014年 / 88卷 / 01期
基金：
英国生物技术与生命科学研究理事会;
关键词：
VESICULAR STOMATITIS-VIRUS; NUCLEOCAPSID PROTEIN; OLIGOMERIZATION DOMAIN; P-PROTEIN; POLYMERASE; MODEL;
D O I：
10.1128/JVI.02294-13
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
The Nipah virus phosphoprotein (P) is multimeric and tethers the viral polymerase to the nucleocapsid. We present the crystal structure of the multimerization domain of Nipah virus P: a long, parallel, tetrameric, coiled coil with a small, alpha-helical cap structure. Across the paramyxoviruses, these domains share little sequence identity yet are similar in length and structural organization, suggesting a common requirement for scaffolding or spatial organization of the functions of P in the virus life cycle.
引用
收藏
页码：758 / 762
页数：5
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