Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95866
Title: Structure of the C-terminal domain of the multifunctional ICP27 protein from herpes simplex virus 1
Authors: Nordlund, Par
Patel, Vidhi
Dahlroth, Sue-Li
Rajakannan, Venkatachalam
Ho, Hai Ting
Cornvik, Tobias
Keywords: DRNTU::Science::Biological sciences::Biochemistry
Issue Date: 2015
Source: 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.
Series/Report no.: Journal of virology
Abstract: 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.
URI: https://hdl.handle.net/10356/95866
http://hdl.handle.net/10220/38454
ISSN: 1098-5514
DOI: 10.1128/JVI.00441-15
Rights: © 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.
Fulltext Permission: open
Fulltext Availability: With Fulltext
Appears in Collections:SBS Journal Articles

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