Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1
Herpesviruses are nuclear-replicating viruses that have successfully evolved to evade the immune system of humans, establishing lifelong infections. ICP27 from herpes simplex virus is a multifunctional regulatory protein that is functionally conserved in all known human herpesviruses. It has the p...
Saved in:
Main Authors: | , , , , , |
---|---|
Other Authors: | |
Format: | Article |
Language: | English |
Published: |
2015
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/95866 http://hdl.handle.net/10220/38454 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
id |
sg-ntu-dr.10356-95866 |
---|---|
record_format |
dspace |
spelling |
sg-ntu-dr.10356-958662023-02-28T16:56:24Z Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 Nordlund, Par Patel, Vidhi Dahlroth, Sue-Li Rajakannan, Venkatachalam Ho, Hai Ting Cornvik, Tobias Dermody, T. S. School of Biological Sciences DRNTU::Science::Biological sciences::Biochemistry Herpesviruses are nuclear-replicating viruses that have successfully evolved to evade the immune system of humans, establishing lifelong infections. ICP27 from herpes simplex virus is a multifunctional regulatory protein that is functionally conserved in all known human herpesviruses. It has the potential to interact with an array of cellular proteins, as well as intronless viral RNAs. ICP27 plays an essential role in viral transcription, nuclear export of intronless RNAs, translation of viral transcripts, and virion host shutoff function. It has also been implicated in several signaling pathways and the prevention of apoptosis. Although much is known about its central role in viral replication and infection, very little is known about the structure and mechanistic properties of ICP27 and its homologs. We present the first crystal structure of ICP27 C-terminal domain at a resolution of 2.0 Å. The structure reveals the C-terminal half of ICP27 to have a novel fold consisting of -helices and long loops, along with a unique CHCC-type of zinc-binding motif. The two termini of this domain extend from the central core and hint to possibilities of making interactions. ICP27 essential domain is capable of forming self-dimers as seen in the structure, which is confirmed by analytical ultracentrifugation study. Preliminary in vitro phosphorylation assays reveal that this domain may be regulated by cellular kinases. Published version 2015-08-18T07:52:30Z 2019-12-06T19:22:29Z 2015-08-18T07:52:30Z 2019-12-06T19:22:29Z 2015 2015 Journal Article Patel, V., Dahlroth, S. L., Rajakannan, V., Ho, H. T., Cornvik, T.,& Nordlund, P. (2015). Structure of the C-Terminal Domain of the Multifunctional ICP27 Protein from Herpes Simplex Virus 1. Journal of Virology, 89(17), 8828-8839. 1098-5514 https://hdl.handle.net/10356/95866 http://hdl.handle.net/10220/38454 10.1128/JVI.00441-15 26085142 en Journal of virology © 2015 [American Society for Microbiology] This paper was published in [Journal of Virology] and is made available as an electronic reprint (preprint) with permission of [American Society for Microbiology]. The published version is available at: [http://dx.doi.org/10.1128/JVI.00441-15]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. 12 p. application/pdf |
institution |
Nanyang Technological University |
building |
NTU Library |
continent |
Asia |
country |
Singapore Singapore |
content_provider |
NTU Library |
collection |
DR-NTU |
language |
English |
topic |
DRNTU::Science::Biological sciences::Biochemistry |
spellingShingle |
DRNTU::Science::Biological sciences::Biochemistry Nordlund, Par Patel, Vidhi Dahlroth, Sue-Li Rajakannan, Venkatachalam Ho, Hai Ting Cornvik, Tobias Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
description |
Herpesviruses are nuclear-replicating viruses that have successfully evolved to evade the immune system of humans, establishing
lifelong infections. ICP27 from herpes simplex virus is a multifunctional regulatory protein that is functionally conserved in
all known human herpesviruses. It has the potential to interact with an array of cellular proteins, as well as intronless viral
RNAs. ICP27 plays an essential role in viral transcription, nuclear export of intronless RNAs, translation of viral transcripts, and
virion host shutoff function. It has also been implicated in several signaling pathways and the prevention of apoptosis. Although
much is known about its central role in viral replication and infection, very little is known about the structure and mechanistic
properties of ICP27 and its homologs. We present the first crystal structure of ICP27 C-terminal domain at a resolution of 2.0 Å.
The structure reveals the C-terminal half of ICP27 to have a novel fold consisting of -helices and long loops, along with a
unique CHCC-type of zinc-binding motif. The two termini of this domain extend from the central core and hint to possibilities
of making interactions. ICP27 essential domain is capable of forming self-dimers as seen in the structure, which is confirmed by
analytical ultracentrifugation study. Preliminary in vitro phosphorylation assays reveal that this domain may be regulated by
cellular kinases. |
author2 |
Dermody, T. S. |
author_facet |
Dermody, T. S. Nordlund, Par Patel, Vidhi Dahlroth, Sue-Li Rajakannan, Venkatachalam Ho, Hai Ting Cornvik, Tobias |
format |
Article |
author |
Nordlund, Par Patel, Vidhi Dahlroth, Sue-Li Rajakannan, Venkatachalam Ho, Hai Ting Cornvik, Tobias |
author_sort |
Nordlund, Par |
title |
Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
title_short |
Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
title_full |
Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
title_fullStr |
Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
title_full_unstemmed |
Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1 |
title_sort |
structure of the c-terminal domain of the multifunctional icp27 protein from herpes simplex virus 1 |
publishDate |
2015 |
url |
https://hdl.handle.net/10356/95866 http://hdl.handle.net/10220/38454 |
_version_ |
1759858258889146368 |