SEQUENCE-STRUCTURE AND HOMOLOGY MODELING OF ICOSAHEDRAL VIRUS CAPSIDS

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。对无包膜球形病毒衣壳蛋白的序列变异和结构相似性进行了系统分析。对9个病毒科的95个外壳蛋白亚基进行的家族内分析表明，尽管存在较大的序列差异(0-97%)，但来自同一家族的VCP在结构上与RMSD有较大程度的相似性，范围为0？3？这清楚地表明，每个家庭中的VCP之间的核心结构是保守的。此外，我们还从核心、界面和表面残基三个方面分析了氨基酸的保守性。毫不奇怪，溶剂可及(表面)残基与溶剂不可及(核心和界面)残基相比不那么保守。尽管将病毒分为植物和非植物病毒家族表现出相似的序列保守模式，但与非植物病毒相比，植物病毒表面暴露残基的序列变异相对较小。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A systematic analysis of sequence variation and structural similarity in viral capsid proteins (VCPs) of non-enveloped, spherical viruses was explored. Intra family analysis of 95 coat protein subunits from 9 virus families suggest that remarkably the VCPs from the same family display greater degree of structural similarity with RMSDs ranging from 0 ¿ 3 ¿ in spite of broad sequence variation (0-97%). This clearly points to the conservation of core structure among VCPs within each family. Furthermore, we analyzed the conservation of amino acids in terms of core, interface and surface lying residues. Not surprisingly, the solvent accessible (surface) residues are less conserved compared to solvent inaccessible (core and interface) residues. Even though, grouping of viruses into plant and non-plant virus families showed similar pattern of sequence conservation, the plant viruses appear to have relatively less variation in the sequence of surface exposed residues compared to non-plant viruses.