XRAY DIFFRACTION OF CD45 CRYSTALS

CD45 晶体的 X 射线衍射

• 批准号: 6586725
• 负责人: ROBERT J FLETTERICK
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586725
• 关键词: bioimaging /biomedical imaging; biomaterials; biomedical resource; proteins; radiography; structural biology

The 3-dimensional structure of the wild type R subunit will provide important information on how the two monomers are relatively oriented to each other, how the protein dimerizies and how the hinge region folds, which is totally disordered in the deletion mutant structure. This dimerization domain also provides a docking site for anchoring the holoenzyme to a variety of scaffolding proteins both in cytoplasm and the nucleus. The crystals of mutant R subunits have defects in their cAMP binding sites. Their structures at high resolution are essential for defining the molecular features of these cAMP binding sites and for understanding the conformational changes which are induced by cAMP binding.

野生型 R 亚基的 3 维结构将 提供有关两个单体相对关系的重要信息 彼此定向，蛋白质如何二聚化以及铰链如何 区域折叠，在缺失突变体中完全无序 结构。 该二聚化结构域还提供了一个对接位点 将全酶锚定到多种支架蛋白上 细胞质和细胞核。 突变R亚基的晶体具有 cAMP 结合位点缺陷。 他们的结构高 分辨率对于定义这些分子特征至关重要 cAMP 结合位点并用于了解构象变化 这是由 cAMP 结合诱导的。