دورية أكاديمية
Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein.
| العنوان: | Structural Features of the Peptide Homologous to 6-25 Fragment of Influenza A PB1 Protein. |
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| المؤلفون: | Egorov VV; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia., Matusevich OV; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Faculty of Chemistry, Saint Petersburg State University, Saint Petersburg 198504, Russia., Shaldzhyan AA; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Skvortsov AN; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Zabrodskaya YA; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Garmay YP; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia ; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia., Landa SB; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia., Lebedev DV; Department of Molecular and Radiation Biophysics, Kurchatov Institute, FSBI St. Petersburg Nuclear Physics Institute, Orlova Roscha, Gatchina 188300, Russia., Zarubayev VV; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Sirotkin AK; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Vasin AV; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia., Kiselev OI; Department of Molecular Virology, FSBI Research Institute of Influenza, Ministry of Health of the Russian Federation, 15/17, Professor Popova Street, Saint Petersburg 197376, Russia. |
| المصدر: | International journal of peptides [Int J Pept] 2013; Vol. 2013, pp. 370832. Date of Electronic Publication: 2013 Dec 24. |
| نوع المنشور: | Journal Article |
| اللغة: | English |
| بيانات الدورية: | Publisher: Hindawi Pub. Corp Country of Publication: United States NLM ID: 101526297 Publication Model: Print-Electronic Cited Medium: Print ISSN: 1687-9767 (Print) Linking ISSN: 16879767 NLM ISO Abbreviation: Int J Pept Subsets: PubMed not MEDLINE |
| أسماء مطبوعة: | Original Publication: New York, NY : Hindawi Pub. Corp. |
| مستخلص: | 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. |
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| تواريخ الأحداث: | Date Created: 20140124 Date Completed: 20140123 Latest Revision: 20211021 |
| رمز التحديث: | 20231215 |
| مُعرف محوري في PubMed: | PMC3886529 |
| DOI: | 10.1155/2013/370832 |
| PMID: | 24454411 |
| قاعدة البيانات: | MEDLINE |
Full Text Finder | تدمد: | 1687-9767 |
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| DOI: | 10.1155/2013/370832 |