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

这个子项目是许多利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 cAMP对蛋白激酶A（PKA）的激活是一个多步骤的过程，涉及cAMP与R亚基中两个不同位点的顺序结合，以及R中结构变化的结果序列，其将C亚基从抑制状态释放。在激活过程中发生的结构变化的性质知之甚少。我们建议做试点时间分辨SAXS实验，以遵循PKA与cAMP混合后发生的溶液结构变化的时间过程。

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.