Polymerase basic protein 2
Also known as: PB2
Function
Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS.
Classification
- Family (Pfam)
- PF20947 Flu_PB2_1st, PF20948 Flu_PB2_2nd, PF20949 Flu_PB2_3rd, PF20950 Flu_PB2_4th, PF00604 Flu_PB2_5th, PF20951 Flu_PB2_6th, PF20952 Flu_PB2_7th
- InterPro
- Flu_PB2_2nd, Flu_PB2_6th, Flu_PB2_C, Flu_PB2_CAP-bd, Flu_PB2_middle, Flu_PB2_N, INV_PB2, PB2_helical, PDB2_C
- Functional cluster
- Mixed Regulatory & Membrane Proteins
Experimental structures · PDB · 10
- 2ZTT X-ray 2.10A
- 3A1G X-ray 1.70A
- 3CW4 X-ray 2.70A
- 3WI0 X-ray 2.00A
- 3WI1 X-ray 1.93A
- 4ENF X-ray 1.32A
- 4J2R X-ray 2.42A
- 4U6O X-ray 1.30A
- 7JYW X-ray 2.90A
- 7JYX X-ray 2.95A
A predicted model is available from AlphaFold.
Gene Ontology · 13
- GO:0005576 extracellular region
- GO:0033650 host cell mitochondrion
- GO:0042025 host cell nucleus
- GO:0044423 virion component
- GO:0003723 RNA binding
- GO:0003968 RNA-directed RNA polymerase activity
- GO:0006370 7-methylguanosine mRNA capping
- GO:0075526 cap snatching
- GO:0006351 DNA-templated transcription
- GO:0039545 symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity
- GO:0039657 symbiont-mediated suppression of host gene expression
- GO:0039523 symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity
- GO:0039694 viral RNA genome replication
Drugs targeting this protein · 2
- FAVIPIRAVIR inhibitor
- PIMODIVIR inhibitor
Related proteins · sequence + function similarity
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
- Polymerase basic protein 2 1.00
Co-cited proteins · studied together in the literature
- Polymerase acidic protein 1 shared papers
- Polymerase basic protein 2 1 shared papers
- PB2-S1 3 shared papers
- Protein PA-X 3 shared papers
- Polymerase acidic protein 4 shared papers
- RNA-directed RNA polymerase catalytic subunit 3 shared papers
- Hemagglutinin 2 shared papers
- Nucleoprotein 2 shared papers
- Neuraminidase 2 shared papers
- Nuclear export protein 2 shared papers
- Matrix protein 2 2 shared papers
- Non-structural protein 1 2 shared papers
Literature · 15 cited papers
- Comparative influenza protein interactomes identify the role of plakophilin 2 in virus restriction. Nat. Commun. · 2017
- An important amino acid in nucleoprotein contributes to influenza A virus replication by interacting with polymerase PB2. Virology · 2014
- Crystallization and preliminary X-ray diffraction studies of a surface mutant of the middle domain of PB2 from human influenza A (H1N1) virus. Acta Crystallogr. F · 2014
- Conformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virus. PLoS ONE · 2013
- Structural and functional characterization of K339T substitution identified in the PB2 subunit cap-binding pocket of influenza A virus. J. Biol. Chem. · 2013
- Influenza A polymerase subunit PB2 possesses overlapping binding sites for polymerase subunit PB1 and human MAVS proteins. Virus Res. · 2013
- Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627. PLoS ONE · 2012
- The PB2 subunit of the influenza virus RNA polymerase affects virulence by interacting with the mitochondrial antiviral signaling protein and inhibiting expression of beta interferon. J. Virol. · 2010
- Structural basis of the influenza A virus RNA polymerase PB2 RNA-binding domain containing the pathogenicity-determinant lysine 627 residue. J. Biol. Chem. · 2009
- Role of the influenza virus heterotrimeric RNA polymerase complex in the initiation of replication. J. Gen. Virol. · 2006
- Characterization of a mitochondrial-targeting signal in the PB2 protein of influenza viruses. Virology · 2006
- The PA subunit is required for efficient nuclear accumulation of the PB1 subunit of the influenza A virus RNA polymerase complex. J. Virol. · 2004
- … and 3 more in the literature graph
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