Cargando…
Molecular basis of host-adaptation interactions between influenza virus polymerase PB2 subunit and ANP32A
Avian influenza polymerase undergoes host adaptation in order to efficiently replicate in human cells. Adaptive mutants are localised on the C-terminal (627-NLS) domains of the PB2 subunit. In particular, mutation of PB2 residue 627 from E to K rescues polymerase activity in mammalian cells. A host...
Autores principales: | Camacho-Zarco, Aldo R., Kalayil, Sissy, Maurin, Damien, Salvi, Nicola, Delaforge, Elise, Milles, Sigrid, Jensen, Malene Ringkjøbing, Hart, Darren J., Cusack, Stephen, Blackledge, Martin |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7374565/ https://www.ncbi.nlm.nih.gov/pubmed/32694517 http://dx.doi.org/10.1038/s41467-020-17407-x |
Ejemplares similares
-
Multivalent Dynamic
Colocalization of Avian Influenza
Polymerase and Nucleoprotein by Intrinsically Disordered ANP32A Reveals
the Molecular Basis of Human Adaptation
por: Camacho-Zarco, Aldo R., et al.
Publicado: (2023) -
Investigating the Role of Large-Scale Domain Dynamics in Protein-Protein Interactions
por: Delaforge, Elise, et al.
Publicado: (2016) -
NMR Provides Unique Insight into the Functional Dynamics
and Interactions of Intrinsically Disordered Proteins
por: Camacho-Zarco, Aldo R., et al.
Publicado: (2022) -
Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid assembly
por: Guseva, Serafima, et al.
Publicado: (2020) -
Self‐Assembly of Measles Virus Nucleocapsid‐like Particles: Kinetics and RNA Sequence Dependence
por: Milles, Sigrid, et al.
Publicado: (2016)