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

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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.