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Journal article

Crystal structure of the Herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodeling.

Abstract:

Although nucleo-cytoplasmic transport is typically mediated through nuclear pore complexes, herpesvirus capsids exit the nucleus via a unique vesicular pathway. Together, the conserved herpesvirus proteins pUL31 and pUL34 form the heterodimeric nuclear egress complex (NEC), which, in turn, mediates the formation of tight-fitting membrane vesicles around capsids at the inner nuclear membrane. Here, we present the crystal structure of the pseudorabies virus NEC. The structure revealed that a zi...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.celrep.2015.11.008

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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Biology
Role:
Author
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São Paulo Research Foundation More from this funder
Max Planck Society More from this funder
Publisher:
Elsevier Publisher's website
Journal:
Cell reports Journal website
Volume:
13
Issue:
12
Pages:
2645-2652
Publication date:
2015-12-16
DOI:
EISSN:
2211-1247
ISSN:
2211-1247
URN:
uuid:c2748706-a680-4788-b66c-da69bd008cb6
Source identifiers:
587363
Local pid:
pubs:587363
Language:
English

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