| Autor: |
Egorov, Vladimir V., Matusevich, Oleg V., Shaldzhyan, Aram A., Skvortsov, Alexey N., Zabrodskaya, Yana A., Garmay, Yuri P., Landa, Sergey B., Lebedev, Dmitry V., Zarubayev, Vladimir V., Sirotkin, Alexey K., Vasin, Andrey V., Kiselev, Oleg I. |
| Předmět: |
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| Zdroj: |
International Journal of Peptides; 2013, p1-5, 5p |
| Abstrakt: |
A mirror-symmetry motif was discovered in the N-terminus of the influenza virus PB1 protein. Structure of peptide comprised of the corresponding part of PB1 (amino acid residues 6-25) was investigated by circular dichroism and in silico modeling. We found that peptide PB1 (6-25) in solution assumes beta-hairpin conformation. A truncated peptide PB1 (6-13), containing only half of the mirror-symmetry motif, appeared to stabilize the beta-structure of the original peptide and, at high concentrations, was capable of reacting with peptide to form insoluble aggregates in vitro. Ability of PB1 (6-13) peptide to interact with the N-terminal domain of PB1 protein makes it a potential antiviral agent that inhibits PA-PB1 complex formation by affecting PB1 N-terminus structure. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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