Structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F21%3A00536615" target="_blank" >RIV/61388963:_____/21:00536615 - isvavai.cz</a>
Alternative codes found
RIV/68378050:_____/21:00544819 RIV/00216208:11110/21:10425868 RIV/00216208:11310/21:10425868
Result on the web
<a href="https://doi.org/10.1016/j.antiviral.2020.104971" target="_blank" >https://doi.org/10.1016/j.antiviral.2020.104971</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.antiviral.2020.104971" target="_blank" >10.1016/j.antiviral.2020.104971</a>
Alternative languages
Result language
angličtina
Original language name
Structural characterization of the interaction between the C-terminal domain of the influenza polymerase PA subunit and an optimized small peptide inhibitor
Original language description
Influenza viruses can cause severe respiratory infections in humans, leading to nearly half a million deaths worldwide each year. Improved antiviral drugs are needed to address the threat of development of novel pandemic strains. Current therapeutic interventions target three key proteins in the viral life cycle: neuraminidase, the M2 channel and RNA-dependent-RNA polymerase. Protein-protein interactions between influenza polymerase subunits are potential new targets for drug development. Using a newly developed assay based on AlphaScreen technology, we screened a peptide panel for protein-protein interaction inhibitors to identify a minimal PB1 subunit-derived peptide that retains high inhibition potential and can be further modified. Here, we present an X-ray structure of the resulting decapeptide bound to the C-terminal domain of PA polymerase subunit from pandemic isolate A/California/07/2009 H1N1 at 1.6 Å resolution and discuss its implications for the design of specific, potent influenza polymerase inhibitors.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Antiviral Research
ISSN
0166-3542
e-ISSN
1872-9096
Volume of the periodical
185
Issue of the periodical within the volume
Jan
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
7
Pages from-to
104971
UT code for WoS article
000604747500003
EID of the result in the Scopus database
2-s2.0-85096015372