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. Author manuscript; available in PMC: 2022 Sep 3.
Published in final edited form as: J Mol Biol. 2021 Jul 3;433(18):167123. doi: 10.1016/j.jmb.2021.167123

Figure 1. Structural and kinetic characterization of PKA-CE31V.

Figure 1.

(A) X-ray structure of PKA-C bound to endogenous inhibitor, PKI (PDB: 1ATP) highlighting important structural elements and locations of Cushing’s syndrome mutations in relation to E31V. (B) Steady state phosphorylation kinetics of PKA-CE31V with Kemptide. (C) CONCISE analysis on the apo, ATPγN-, ADP- and ATPγN/PKI-bound forms of PKA-CWT (opaque gaussian) and PKA-CE31V (outlined gaussian). Note that the probability distribution of PKA-CWT when bound to ATPγN (yellow) and ADP (orange) are overlapping.