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腺病毒5型蛋白IX的C末端结构域在衣壳小面上组装成反平行结构。

The C-terminal domains of adenovirus serotype 5 protein IX assemble into an antiparallel structure on the facets of the capsid.

作者信息

Fabry Céline M S, Rosa-Calatrava Manuel, Moriscot Christine, Ruigrok Rob W H, Boulanger Pierre, Schoehn Guy

机构信息

Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, Grenoble cedex 9, France.

出版信息

J Virol. 2009 Jan;83(2):1135-9. doi: 10.1128/JVI.01808-08. Epub 2008 Nov 12.

DOI:10.1128/JVI.01808-08
PMID:19004948
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2612400/
Abstract

Adenovirus serotype 5 protein IX (pIX) has two domains connected by a flexible linker. Three N-terminal domains form triskelions on the capsid facets that cement hexons together, and the C-terminal domains of four monomers form complexes toward the facet periphery. Here we present a cryoelectron microscopy structure of recombinant adenovirus with a peptide tag added to the C terminus of pIX. The structure, made up by several C termini of pIX, is longer at both ends than the wild-type protein, and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C termini associate in an antiparallel manner.

摘要

腺病毒5型蛋白IX（pIX）有两个由柔性连接子相连的结构域。三个N端结构域在衣壳小平面上形成三聚体，将六邻体固定在一起，四个单体的C端结构域朝向小平面周边形成复合物。在此，我们展示了一种在pIX的C端添加了肽标签的重组腺病毒的冷冻电子显微镜结构。该结构由几个pIX的C端组成，两端比野生型蛋白更长，针对该标签的Fab片段与寡聚体的两端结合，表明pIX的C端以反平行方式缔合。

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本文引用的文献

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