- Abstract:
-
Influenza virus RNA polymerase (FluPol), a heterotrimer composed of PB1, PB2, and PA subunits (P3 in influenza C), performs both transcription and replication of the viral RNA genome. For transcription, FluPol interacts with the C-terminal domain (CTD) of RNA polymerase II (Pol II), which enables FluPol to snatch capped RNA primers from nascent host RNAs. Here, we describe the co-crystal structure of influenza C virus polymerase (FluPolC) bound to a Ser5-phosphorylated CTD (pS5-CTD) peptide. ...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Version:
- Publisher's version
- Files:
-
-
(pdf, 3.8MB)
-
(pdf, 3.9MB)
-
- Publisher copy:
- 10.1016/j.molcel.2018.05.011
-
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- Publisher:
- Elsevier Publisher's website
- Journal:
- Molecular Cell Journal website
- Volume:
- 70
- Issue:
- 6
- Pages:
- 1101–1110.e4
- Publication date:
- 2018-06-14
- Acceptance date:
- 2018-05-08
- DOI:
- EISSN:
-
1097-4164
- ISSN:
-
1097-2765
- Pubs id:
-
pubs:853057
- URN:
-
uri:028fb37f-abda-4154-9f71-811ded69fcbf
- UUID:
-
uuid:028fb37f-abda-4154-9f71-811ded69fcbf
- Local pid:
- pubs:853057
- Copyright holder:
- © 2018 The Author(s). Published by Elsevier Inc.
- Copyright date:
- 2018
- Notes:
-
This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
Note: an erratum exists for this article, originally published and available at: https://doi.org/10.1016/j.molcel.2018.10.005
Journal article
A mechanism for the activation of the influenza virus transcriptase
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