CAMP DEPENDENT PROTEIN KINASE HOLOENZYME COMPLEX

CAMP 依赖性蛋白激酶全酶复合物

• 批准号: 6119541
• 负责人: XIAODONG CHENG
• 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/6119541
• 关键词: biomaterials; proteins; structural biology

cAMP-dependent protein kinase (cAPK) plays critical roles in different cellular functions. The crystal structure of the catalytic subunit of cAPK is the first protein kinase structure determined and has served as a prototype for the entire protein kinase family, one of the largest protein family. We have also solved the crystal structure of a deletion regulatory subunit using the synchrotron radiation facility at SSRL and this structure has provided valuable insights into how cAPK interact with the second messenger, cAMP. We are now successful in producing crystals of a cAPK holoenzyme complex formed by the catalytic subunit and a deletion regulatory subunit and have collected a complete data set at 3.4 E at home source. Our goal of this proposal is to solve the holoenzyme complex structure at high resolution. Synchrotron radiation at SSRL will allow the collection of the highest possible resolution data, which is necessary for accurate structure determination at high resolution. Solving the holoenzyme complex structure will help us understand the mechanism of cAPK regulation and function.

cAMP依赖性蛋白激酶（cAPK）在 不同的细胞功能 催化剂的晶体结构 cAPK的亚基是确定的第一个蛋白激酶结构， 作为整个蛋白激酶家族的原型， 最大的蛋白质家族 我们还解决了晶体结构 缺失调节亚基的同步辐射 SSRL的设施，这种结构提供了宝贵的见解 cAPK如何与第二信使cAMP相互作用。 我们现在 成功地生产了cAPK全酶复合物的晶体， 由催化亚基和缺失调节亚基组成， 在3.4E的家庭来源收集了完整的数据集。 的目标 该方案是为了解决全酶复合物结构在高 分辨率 SSRL的同步辐射将允许收集 尽可能高的分辨率数据，这是必要的 以高分辨率进行精确的结构测定。 解决 全酶复合物的结构将有助于我们了解 cAPK调节和功能。