SEQUENCE-STRUCTURE AND HOMOLOGY MODELING OF ICOSAHEDRAL VIRUS CAPSIDS

二十面体病毒衣壳的序列结构和同源性建模

• 批准号: 7957347
• 负责人: VIJAY S REDDY
• 金额: $ 3.65万
• 依托单位: UNIVERSITY OF MICHIGAN AT ANN ARBOR
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-09-01 至 2010-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7957347
• 关键词: Amino Acids; Capsid; Capsid Proteins; Classification; Computer Retrieval of Information on Scientific Projects Database; Family; Funding; Grant; Grouping; Homology Modeling; Institution; Pattern; Plant Viruses; Plants; Protein Subunits; Research; Research Personnel; Resources; Sequence Analysis; Solvents; Source; Structure; Surface; United States National Institutes of Health; Variant; Viral; Virus; multi-scale modeling; structural biology; tool

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.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以出现在其他 CRISP 条目中 列出的机构是。 对于中心来说，它不一定是研究者的机构。 对无包膜球形病毒的病毒衣壳蛋白 (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了科内分析，表明来自同一科的 VCP 表现出更大的程度。结构相似性与 RMSD 范围为 0 3 ¿尽管存在广泛的序列变异（0-97%），这清楚地表明每个家族内VCP之间的核心结构的保守性，此外，我们分析了核心、界面和表面残基的氨基酸保守性。 ，与溶剂不可接近（核心和界面）残基相比，溶剂可接近（表面）残基的保守性较低。尽管将病毒分为植物和非植物病毒家族，显示出相似的序列保守模式，但植物病毒似乎具有相对较高的序列保守性。表面顺序的变化较小与非植物病毒相比，暴露的残留物。