CRYSTALLOGRAPHIC STUDIES OF VIRULENCE FACTORS, HOST-PATHOGEN INTERACTIONS, AND O

毒力因子、宿主-病原体相互作用和 O 的晶体学研究

• 批准号: 8170178
• 负责人: LIEH YOON LOW
• 金额: $ 0.47万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170178
• 关键词: Collection; Collimator; Complex; Computer Retrieval of Information on Scientific Projects Database; Data; Dedications; Disease; Drug Design; Funding; Future; Grant; Immune; Inflammation; Institution; Integration Host Factors; Laboratories; Phase; Play; Proteins; Reporting; Research; Research Personnel; Resolution; Resources; Role; Science; Source; Structure; Support Groups; Therapeutic; United States National Institutes of Health; Virulence Factors; Work; anthrax toxin; cell motility; design; inhibitor/antagonist; neutralizing antibody; pathogen; programs; structural biology

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. This is a continuing proposal for the Liddington laboratory, describing our overall program in structural biology at the SSRL. The major focuses are anthrax toxin and virulence factors from other high priority pathogens and emerging diseases, and their interactions with host factors, as well as host proteins involved in cell migration and inflammation. The work involves ab initio structure determination by MAD phasing, studies of protein-inhibitor complexes for rational drug design, and complexes with neutralizing antibodies for designing immune therapeutics. I report highlights of our studies for the 2005-2008 period in the context of our earlier work at SSRL, as well as our ongoing and future studies. This work illustrates how the SSRL has played a central and critical role in most aspects of our science ? using its tunability for primary structure determination/phasing; and/or the high brightness, collimation and stability of the SSRL source for the collection of high resolution data from demanding crystals. And all of this made possible and much more pleasant through the dedication of the outstanding User Support Group.

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。 这是对Liddington实验室的持续建议，描述了我们在SSRL的结构生物学的整体计划。主要重点是炭疽毒素和其他高优先级病原体和新兴疾病的毒力因子，以及它们与宿主因子的相互作用，以及参与细胞迁移和炎症的宿主蛋白质。这项工作涉及通过MAD定相的从头计算结构确定，用于合理药物设计的蛋白质抑制剂复合物的研究，以及用于设计免疫疗法的中和抗体复合物。我报告的重点，我们的研究为2005-2008年期间，我们在SSRL的早期工作的背景下，以及我们正在进行和未来的研究。这项工作说明了SSRL如何在我们科学的大多数方面发挥核心和关键作用？利用其可调谐性进行一级结构测定/定相;和/或SSRL源的高亮度、准直和稳定性，用于从要求高的晶体收集高分辨率数据。所有这一切都是通过杰出的用户支持小组的奉献精神而实现的，而且更加令人愉快。