KINETICS OF CAMP-INDUCED STRUCTURAL CHANGES IN PKA BY TR-SAXS

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 CAMP激活蛋白激酶A(PKA)是一个多步骤的过程，包括cAMP与R亚基上两个不同位置的cAMP顺序结合，以及由此产生的R结构变化序列，将C亚基从抑制状态释放出来。人们对激活过程中发生的结构变化的性质知之甚少。我们建议进行中试时间分辨SAXS实验，以跟踪PKA与cAMP混合后溶液结构变化的时间进程。

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. The activation of protein kinase A (PKA) by cAMP is a multi-step process involving sequential cAMP binding to two different sites in the R subunit, and a resultant sequence of structural changes in R that release the C subunit from an inhibited state. The nature of the structural changes that occur during activation are poorly understood. We propose to do pilot time-resolved SAXS experiments to follow the time course of solution structural changes that occur after mixing PKA with cAMP.