SEQUENCE-STRUCTURE AND HOMOLOGY MODELING OF ICOSAHEDRAL VIRUS CAPSIDS

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 对无包膜球形病毒衣壳蛋白（VCP）的序列变异和结构相似性进行了系统分析。对来自9个病毒科的95个外壳蛋白亚基进行的科内分析表明，来自同一个病毒科的VCPs在结构上有很大的相似性，RMSDs在0  尽管存在广泛的序列变异（0-97%），但仍为3 º。这清楚地表明，每个家族内VCP之间的核心结构是保守的。此外，我们分析了氨基酸的保守性的核心，界面和表面躺残基。毫不奇怪，与溶剂不可及的（核心和界面）残基相比，溶剂可及的（表面）残基保守性较低。尽管将病毒分组为植物和非植物病毒家族显示出相似的序列保守模式，但与非植物病毒相比，植物病毒似乎在表面暴露残基的序列中具有相对较少的变异。

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.