- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 3.4MB)
-
- Publisher copy:
- 10.1016/j.celrep.2015.11.008
-
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- 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
- Copyright holder:
- Zeev-Ben-Mordehai et al.
- Copyright date:
- 2015
- Notes:
- Copyright © 2015 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Journal article
Crystal structure of the Herpesvirus nuclear egress complex provides insights into inner nuclear membrane remodeling.
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São Paulo Research Foundation
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Max Planck Society
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