SMALL ANGLE SCATTERING STUDIES OF CAMP & CGMP DEPENDENT PROTEIN KINASES

CAMP的小角散射研究

• 批准号: 6586793
• 负责人: JILL TREWHELLA
• 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/6586793
• 关键词: bioimaging /biomedical imaging; biomedical resource; human tissue; proteins; radiography; structural biology

Small-angle scattering data from type Ia cGMP-dependent protein kinase (PKG) titrated with cGMP (1 through 13 molar equivalents) shows a large conformational change induced by cGMP-binding. PKG is a dimer with a regulatory and catalytic domain within each monomer component. There is one 'slow' and one 'fast' cGMP binding site on each monomer. A P(r) analysis of the scattering data indicates that the conformational change involves a shift of the molecular mass away from the center of the molecule, possibly due to the movement of the regulatory domain away from the catalytic domain. The radius of gyration of PKG increases dramatically by 30% from 45.4 to 59.4 E upon addition of cGMP. It appears that the 4 cGMP binding sites per PKG may only need to be partially saturated to see the full confromational change. Further study is underway to characterize the exact role of the slow and fast cGMP-binding sites.

Ia型cGMP依赖蛋白的小角散射数据 用cGMP(1至13摩尔当量)滴定的蛋白激酶(PKG)显示 CGMP结合引起的大的构象变化。PKG是一种二聚体 在每个单体组分中具有调节和催化结构域。 每个单体上都有一个“慢”和一个“快”cGMP结合位点。 对散射数据的P(R)分析表明， 构象变化涉及分子质量从 分子的中心，可能是由于分子的运动 远离催化结构域的调控结构域。星体的半径 PKG的自转速度从45.4E急剧增加到59.4E 添加cGMP。似乎每个PKG有4个cGMP结合位点 可能只需要部分饱和即可看到完整的 变化。进一步的研究正在进行中，以确定其确切的作用 慢速和快速cGMP结合位点。