Bogacheva E N, Dolgov A A, Chulichkov A L, Shishkov A V, Ksenofontov A L, Fedorova N V, Baratova L A
Bioorg Khim. 2012 Jan-Feb;38(1):70-7. doi: 10.1134/s1068162012010037.
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.
利用氚平面成像技术研究了甲型流感病毒A/波多黎各/8/34（PR8，H1N1亚型）M1蛋白在溶液中的空间结构以及病毒粒子的组成。使用特殊的空间结构建模算法来模拟实验，以及一组预测蛋白质二级结构和无序区域的算法。利用Rosetta程序对三级结构进行了优化。为了比较溶液中和病毒粒子中的结构，还使用了NM结构域的X射线衍射数据。在溶液中的蛋白质结构与晶体结构的主要差异出现在N结构域和M结构域的接触区域，在结晶状态下它们堆积得更为紧密。标记最大值的位置几乎与通过生物信息学分析预测的蛋白质无结构区域相同。这些区域集中在C结构域以及M、N和C结构域之间的环区。分析超速离心和动态激光光散射证实了氚平面成像的数据。发现了溶液中M1蛋白异常的流体动力学尺寸和低结构化。细胞中蛋白质的多功能性似乎与其可塑性的三级结构有关，这种结构是以与各种分子伙伴接触的无结构区域为代价提供的。
