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Title: Small-angle X-Ray analysis of macromolecular structure: the structure of protein NS2 (NEP) in solution

Abstract

A complex structural analysis of nuclear export protein NS2 (NEP) of influenza virus A has been performed using bioinformatics predictive methods and small-angle X-ray scattering data. The behavior of NEP molecules in a solution (their aggregation, oligomerization, and dissociation, depending on the buffer composition) has been investigated. It was shown that stable associates are formed even in a conventional aqueous salt solution at physiological рН value. For the first time we have managed to get NEP dimers in solution, to analyze their structure, and to compare the models obtained using the method of the molecular tectonics with the spatial protein structure predicted by us using the bioinformatics methods. The results of the study provide a new insight into the structural features of nuclear export protein NS2 (NEP) of the influenza virus A, which is very important for viral infection development.

Authors:
 [1];  [2];  [1];  [3];  [4];  [5];  [4];  [6]
  1. Russian Academy of Sciences, Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” (Russian Federation)
  2. Russian Academy of Sciences, Semenov Institute of Chemical Physics (Russian Federation)
  3. c/o DESY, EMBL, Hamburg Outstation (Germany)
  4. Moscow State University, Belozersky Institute of Physico-Chemical Biology (Russian Federation)
  5. Moscow State University, Faculty of Bioengineering and Bioinformatics (Russian Federation)
  6. Russian Academy of Sciences, Frumkin Institute of Electrochemistry (Russian Federation)
Publication Date:
OSTI Identifier:
22758325
Resource Type:
Journal Article
Journal Name:
Crystallography Reports
Additional Journal Information:
Journal Volume: 62; Journal Issue: 6; Other Information: Copyright (c) 2017 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 1063-7745
Country of Publication:
United States
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; 37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; AGGLOMERATION; AQUEOUS SOLUTIONS; BUFFERS; COMPARATIVE EVALUATIONS; DIMERS; DISSOCIATION; INFLUENZA VIRUSES; MOLECULES; PROTEIN STRUCTURE; PROTEINS; SALTS; SMALL ANGLE SCATTERING; X-RAY DIFFRACTION

Citation Formats

Shtykova, E. V., E-mail: shtykova@ns.crys.ras.ru, Bogacheva, E. N., Dadinova, L. A., Jeffries, C. M., Fedorova, N. V., Golovko, A. O., Baratova, L. A., and Batishchev, O. V.. Small-angle X-Ray analysis of macromolecular structure: the structure of protein NS2 (NEP) in solution. United States: N. p., 2017. Web. doi:10.1134/S1063774517060220.
Shtykova, E. V., E-mail: shtykova@ns.crys.ras.ru, Bogacheva, E. N., Dadinova, L. A., Jeffries, C. M., Fedorova, N. V., Golovko, A. O., Baratova, L. A., & Batishchev, O. V.. Small-angle X-Ray analysis of macromolecular structure: the structure of protein NS2 (NEP) in solution. United States. doi:10.1134/S1063774517060220.
Shtykova, E. V., E-mail: shtykova@ns.crys.ras.ru, Bogacheva, E. N., Dadinova, L. A., Jeffries, C. M., Fedorova, N. V., Golovko, A. O., Baratova, L. A., and Batishchev, O. V.. Wed . "Small-angle X-Ray analysis of macromolecular structure: the structure of protein NS2 (NEP) in solution". United States. doi:10.1134/S1063774517060220.
@article{osti_22758325,
title = {Small-angle X-Ray analysis of macromolecular structure: the structure of protein NS2 (NEP) in solution},
author = {Shtykova, E. V., E-mail: shtykova@ns.crys.ras.ru and Bogacheva, E. N. and Dadinova, L. A. and Jeffries, C. M. and Fedorova, N. V. and Golovko, A. O. and Baratova, L. A. and Batishchev, O. V.},
abstractNote = {A complex structural analysis of nuclear export protein NS2 (NEP) of influenza virus A has been performed using bioinformatics predictive methods and small-angle X-ray scattering data. The behavior of NEP molecules in a solution (their aggregation, oligomerization, and dissociation, depending on the buffer composition) has been investigated. It was shown that stable associates are formed even in a conventional aqueous salt solution at physiological рН value. For the first time we have managed to get NEP dimers in solution, to analyze their structure, and to compare the models obtained using the method of the molecular tectonics with the spatial protein structure predicted by us using the bioinformatics methods. The results of the study provide a new insight into the structural features of nuclear export protein NS2 (NEP) of the influenza virus A, which is very important for viral infection development.},
doi = {10.1134/S1063774517060220},
journal = {Crystallography Reports},
issn = {1063-7745},
number = 6,
volume = 62,
place = {United States},
year = {2017},
month = {11}
}