tailieunhanh - báo cáo khoa hoc : Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium

The structure of the C-terminal domain of the influenza virus A matrix M1 protein, for which X-ray diffraction data were still missing, was studied in acidic solution. Matrix M1 protein was bombarded with thermally-acti-vated tritium atoms, and the resulting intramolecular distribution of the tri-tium label was analyzed to assess the steric accessibility of the amino acid residues in this protein. | IFEBS Journal Spatial structure peculiarities of influenza A virus matrix M1 protein in an acidic solution that simulates the internal lysosomal medium Alexander Shishkov1 Elena Bogacheva1 Natalia Fedorova2 Alexander Ksenofontov2 Gennadii Badun3 Victor Radyukhin2 Elena Lukashina2 Marina Serebryakova4 Alexey Dolgov1 Alexey Chulichkov1 Evgeny Dobrov2 and Lyudmila Baratova2 1 N. N. Semenov Institute of ChemicalPhysics Russian Academy of Sciences Moscow Russia 2 A. N. Belozersky Institute of Physico-ChemicalBiology Moscow State University Russia 3 Department of Chemistry Moscow State University Russia 4 Institute of Physico-ChemicalMedicine FederalAgency for Health Care and SocialDevelopment Moscow Russia Keywords bioinformatics tools influenza A virus matrix M1 protein tritium planigraphy 3D modeling Correspondence L. Baratova Department of Chromatographic Analysis A. N. Belozersky Institute of Physico-ChemicalBiology Moscow State University Leninskie Gory Moscow 119991 Russia Fax 7 495 9393181 Tel 7 495 9395408 E-mail baratova@ Note The present study partly includes recently published preliminary results Ksenofontov AL et al. 2011 Mol Biol Moscow 45 634-640 Received 9 November 2010 revised 16 May 2011 accepted 28 September 2011 doi The structure of the C-terminal domain of the influenza virus A matrix Ml protein for which X-ray diffraction data were still missing was studied in acidic solution. Matrix M1 protein was bombarded with thermally-activated tritium atoms and the resulting intramolecular distribution of the tritium label was analyzed to assess the steric accessibility of the amino acid residues in this protein. This technique revealed that interdomain loops and the C-terminal domain of the protein are the most accessible to labeling with tritium atoms. A model of the spatial arrangement of the C-termi-nal domain of matrix M1 protein was generated using ROSETTA software adjusted to the data obtained by tritium

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