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: 6119408
• 负责人: EDWARD N BAKER
• 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/6119408
• 关键词: hematology; proteins

Hemopexin is a serum glycoprotein which binds the heme released by hemoglobin breakdown 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. The structure of the C-domain is known. 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，其结合由血红素结合蛋白释放的血红素。 血红蛋白分解并通过特定的 受体。 血液结合蛋白由两个结构域组成， 它结合血红素，和一个C-末端结构域， 受体结合 C结构域的结构是已知的。 以来 氨基酸比较表明，这两个结构域可能具有 类似的结构，这使我们能够模拟血红素结合 域 我们有完整分子的晶体，但这些证明 对温度非常敏感，并且很难安装 在毛细血管中成功。 晶体冷冻和使用 SSRL的同步辐射将是唯一的方法， 可以从这些晶体收集数据。