STRUCTURAL STUDIES ON MAMMALIAN BINDING PROTEINS & HEAT STABLE ENZYMES

血凝素是一种血清糖蛋白，它结合由 血红蛋白分解并通过特定的途径将其输送到肝脏 感受器。血凝素由两个结构域组成，一个N-末端结构域 它与血红素结合，以及C-末端结构域，这是 受体结合。C-结构域的结构是已知的。自.以来 氨基酸比较表明，这两个结构域很可能都有 类似的结构，这使我们能够模拟血红素的结合 域。我们有完整分子的晶体，但这些证明 对温度非常敏感，而且很难安装 成功地进入了毛细血管。结晶冷冻及其应用 SSRL的同步辐射将是任何有用的 可以从这些晶体中收集数据。

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.