Crystal Structure of the Nipah Virus Phosphoprotein Tetramerization Domain

被引：67

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

页码：758 / 762

页数：5

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