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.

该副本是利用众多研究子项目之一 由NIH/NCRR资助的中心赠款提供的资源。子弹和 调查员（PI）可能已经从其他NIH来源获得了主要资金， 因此可以在其他清晰的条目中代表。列出的机构是 对于中心，这不一定是调查员的机构。 这是利丁顿实验室的持续提案，描述了我们在SSRL的结构生物学总体计划。主要重点是其他高优先病原体和新兴疾病的炭疽毒素和毒力因子，以及它们与宿主因素的相互作用，以及与细胞迁移和炎症有关的宿主蛋白。这项工作涉及通过疯狂的相分化的从头算结构的确定，对理性药物设计的蛋白质抑制剂复合物的研究以及具有中和抗体设计免疫治疗剂的复合物。我报告了我们在SSRL的早期工作以及我们正在进行的和未来的研究的背景下，在2005-2008期间的研究重点。这项工作说明了SSRL如何在我们科学的大多数方面发挥着重要和关键作用？使用其可调性来确定/相位；和/或SSRL来源的高亮度，准确性和稳定性，用于收集苛刻晶体的高分辨率数据。所有这些使杰出的用户支持小组的奉献精神变得更加令人愉悦。