STRUCTURAL STUDIES ON MAMMALIAN BINDING PROTEINS & HEAT STABLE ENZYMES

哺乳动物结合蛋白的结构研究

• 批准号: 6437560
• 负责人: EDWARD N BAKER
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437560
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; hematology; proteins; radiography; structural biology

Hemopexin is a serum glycoprotein which binds the heme released by hemoglobin breakdown, transport it, and delivers it to the liver via specific receptors. Hemopexin consists of two domains, an N-terminal domain which binds heme, and a C-terminal domain which is essential for receptor binding. Since amino acid comparisons show that both domains are likely to have similar structures, this has enable us to model the heme binding domain. We have crystals of the intact molecule, but these prove to be extremely temperature-sensitive and very difficult to mount successfully in capillaries. Crystal freezing and the use of synchrotron radiation at SSRL will be the only way in which any useful data can be collected from these crystals.

血红素结合蛋白是一种血清糖蛋白，可与血红素结合 血红蛋白分解、运输并通过以下方式输送到肝脏 特定受体。 血红素结合蛋白由两个结构域组成，一个是 N 端 结合血红素的结构域和必需的 C 端结构域 用于受体结合。 由于氨基酸比较表明两者 域可能具有相似的结构，这使我们能够 模拟血红素结合域。 我们有完整的水晶 分子，但这些被证明对温度极其敏感并且 很难在毛细血管中成功安装。 水晶冷冻 SSRL 使用同步加速器辐射将是唯一的方法 可以从这些晶体中收集任何有用的数据。