STRUCTURAL STUDY OF CAMP DEPENDENT PROTEIN KINASE DELETION HOLOENZYME COMPLEX

营依赖性蛋白激酶缺失全酶复合物的结构研究

• 批准号: 6119555
• 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/6119555
• 关键词: biomaterials; proteins

cAMP-dependent protein kinase (cAPK) plays important roles in different celluar 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. We have solved the crystal structure of a deletion regulatory subunit using the synchrotron radiation facility at SSRL. This structure has provided valuable insights into how cAPK interacts with the secondary messenger, cAMP. We are now producing crystals of a deletion cAPK holoenzyme complex formed by the catalytic subunit and the deletion regulatory subunit, delta (1-91)R. This holoenzyme crystal structure will first-time provide detailed information on how the catalytic and regulatory subunits interact thus, help us understand the mechanism of cAPK regulation. The deletion holo-complex crystal diffracted to 3.5 E at home source.

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。 我们 已经解决了缺失调节亚基的晶体结构， 使用SSRL的同步辐射设备。 该结构具有 提供了关于cAPK如何与次要细胞相互作用的宝贵见解， 信使cAMP 我们现在正在生产一种缺失的cAPK晶体 由催化亚基和缺失形成的全酶复合物 调节亚基delta（1-91）R。 这种全酶的晶体结构 将首次提供有关如何催化和 调节亚基相互作用，从而帮助我们了解 cAPK调节。 删除全息复合物晶体衍射到3.5 在家里的来源。