STRUCTURAL STUDIES OF HUMAN & VIRAL RECEPTOR PROTEINS

人体结构研究

• 批准号: 6119394
• 负责人: Theodore S Jardetzky
• 金额: --
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-03-01 至 2000-04-14
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6119394
• 关键词: biomaterials; immunology; inflammation; proteins

The expression of different Fc receptors on discrete cell types allows a combinatorial linkage of the exquisitely sensitive antibody response to cell-mediated immune mechanisms, including cytotoxic, degranulatory and phagocytic reactions. We have obtained diffraction quality crystals for both the IgE-receptor and the IgE-Fc ligand. Elucidation of these structures will provide a new of this important link between antibody specificity and cellular immune responses. Enveloped viruses have evolved intriguing mechanisms for entry into their host cells. The paramyxovirus F protein mediates the fusion of the virus envelope and target cell membrane. Two F-protein fragments assemble into a "post-fusion"structure, which might arise after a triggered conformational change in the intact F protein. The crystals of this F-protein "core" will provide new insights into the fusion mechanisms of the paramyxovirus family.

不同Fc受体在离散细胞类型上的表达 允许组合连接极敏感的抗体 对细胞介导的免疫机制的应答，包括细胞毒性， 脱颗粒和吞噬反应。 我们得到了衍射 IgE受体和IgE-Fc配体的优质晶体。 阐明这些结构将提供一个新的这一重要的 抗体特异性和细胞免疫反应之间的联系。 包膜病毒已经进化出了有趣的机制， 它们的宿主细胞 副粘病毒F蛋白介导的融合 病毒包膜和靶细胞膜。 两个F蛋白片段 组装成一个“后融合”结构，这可能会出现在一个 引发了完整F蛋白的构象变化 晶体 这一F蛋白“核心”将提供新的见解融合 副粘病毒家族的机制。