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

Journal Article · · Crystallography Reports
 [1];  [2];  [3];  [4];  [5];  [4];  [6]
  1. Russian Academy of Sciences, Semenov Institute of Chemical Physics (Russian Federation)
  2. Russian Academy of Sciences, Shubnikov Institute of Crystallography, Federal Scientific Research Centre “Crystallography and Photonics,” (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)

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.

OSTI ID:
22758325
Journal Information:
Crystallography Reports, Vol. 62, Issue 6; Other Information: Copyright (c) 2017 Pleiades Publishing, Inc.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7745
Country of Publication:
United States
Language:
English