Binding interaction between PKA-C and RKIP and its mutant P74L



Kinetical and structural characterization of the interaction between the RAF kinase inhibitor (RKIP) and the cAMP-dependent protein kinase A (PKA-C) by interferometry and nuclear magnetic resonance (NMR) spectroscopy analysis. Together with the analysis performed by Dr. Marsha Rosner's laboratory (University of Chicago), these studies are part of a paper that has been sent to the PNAS journal.

Raw and processed (GraphPad format) for the kinetics of binding between immobilized human PKA-C and RKIPwt obtained by biolayer interferometry analysis (BLItz - ForteBio). NMR chemical perturbation (CSP) analysis of the amide chemical shift of RKIPwt and P74L RKIP mutant in complex with ATPγN-saturatedPKA-C and CSP analysis of the amide chemical shifts of human PKA-C in complex with RKIP, under ATPγN saturating condiction.

Referenced by
Raf Kinase Inhibitory Protein (RKIP) Regulates the cAMP-dependent Protein Kinase Signaling Pathway Through a Positive Feedback loop (sent to the editorial office of PNAS)
Date made availableJan 3 2022
PublisherData Repository for the University of Minnesota
Date of data productionJul 1 2015 - Dec 30 2020

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