Protein kinase inhibitor (PKI) is a 75 residue protein responsible for the inhibition and nuclear export of protein kinase A (PKA). The exportin CRM1 binds the nuclear export signal of PKI and transports the PKI:PKA cargo through a nuclear pore complex. We are interested in investigating the mechanism by which PKI, an intrinsically disordered protein, is involved in the binding and recognition of PKA for inhibition and nuclear export. Our goal is to use NMR to characterize the binding of PKI to PKA, as well as the binding of CRM1 to their complex. To initiate these studies, we optimized the expression and purification of recombinant PKI. We then conducted multi dimensional NMR experiments in order to assign each of the resonances in the HN-HSQC spectrum of PKI. The assignment will be presented. With the assignment we can begin characterizing PKI in complex with the other components of the nuclear export system.

Assignment of the HN-HSQC NMR spectrum of heat stable protein kinase inhibitor (PKI)

249th National Meeting (2015)

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