دورية أكاديمية
[Differences in spatial structures of the influenza virus M1 protein in crystal, solution and virion].
| العنوان: | [Differences in spatial structures of the influenza virus M1 protein in crystal, solution and virion]. |
|---|---|
| المؤلفون: | Bogacheva EN, Dolgov AA, Chulichkov AL, Shishkov AV, Ksenofontov AL, Fedorova NV, Baratova LA |
| المصدر: | Bioorganicheskaia khimiia [Bioorg Khim] 2012 Jan-Feb; Vol. 38 (1), pp. 70-7. |
| نوع المنشور: | English Abstract; Journal Article |
| اللغة: | Russian |
| بيانات الدورية: | Publisher: Nauka Country of Publication: Russia (Federation) NLM ID: 7804941 Publication Model: Print Cited Medium: Print ISSN: 0132-3423 (Print) Linking ISSN: 01323423 NLM ISO Abbreviation: Bioorg Khim Subsets: MEDLINE |
| أسماء مطبوعة: | Original Publication: Moskva, Nauka |
| مواضيع طبية MeSH: | Models, Molecular*, Influenza A Virus, H1N1 Subtype/*chemistry , Viral Matrix Proteins/*chemistry , Virion/*chemistry, Protein Structure, Tertiary ; X-Ray Diffraction |
| مستخلص: | Spatial structure of the influenza virus A/Puerto Rico/8/34 (PR8, subtype H1N1) M1 protein in a solution and composition of the virion was studied by tritium planigraphy technique. The special algorithm for modeling of the spatial structure is used to simulate the experiment, as well as a set of algorithms predicting secondary structure and disordered regions in proteins. Tertiary structures were refined using the program Rosetta. To compare the structures in solution and in virion, also used the X-ray diffraction data for NM-domain. The main difference between protein structure in solution and crystal is observed in the contact region of N- and M-domains, which are more densely packed in the crystalline state. Locations include the maximum label is almost identical to the unstructured regions of proteins predicted by bioinformatics analysis. These areas are concentrated in the C-domain and in the loop regions between the M-, N-, and C-domains. Analytical centrifugation and dynamic laser light scattering confirm data of tritium planigraphy. Anomalous hydrodynamic size, and low structuring of the M1 protein in solution were found. The multifunctionality of protein in the cell appears to be associated with its plastic tertiary structure, which provides at the expense of unstructured regions of contact with various molecules-partners. |
| المشرفين على المادة: | 0 (M1 protein, Influenza A virus) 0 (Viral Matrix Proteins) |
| تواريخ الأحداث: | Date Created: 20120717 Date Completed: 20120912 Latest Revision: 20191027 |
| رمز التحديث: | 20221213 |
| DOI: | 10.1134/s1068162012010037 |
| PMID: | 22792708 |
| قاعدة البيانات: | MEDLINE |
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