Fig. 1: Multiple conformations adopted by the dynamic J-domain alters allosteric binding cooperativity of PKA-C. | Communications Biology

Fig. 1: Multiple conformations adopted by the dynamic J-domain alters allosteric binding cooperativity of PKA-C.

From: Defective internal allosteric network imparts dysfunctional ATP/substrate-binding cooperativity in oncogenic chimera of protein kinase A

Fig. 1

a Overlay of selected snapshots of PKA-CDNAJB1 from the MD trajectories highlighting the ensemble of conformers sampled by the J-domain. b SAXS profiles of PKA-CDNAJB1. Continuous lines show the structural fitting of the experimental SAXS data with the closed (J-domain in, blue), intermediate (green), and extended (J-domain out, magenta) conformations for binary (ATPγN-bound) and ternary (ATPγN/PKI-bound) forms. The conformations are extracted from the MD trajectories. c Corresponding Kratky plot of PKA-CDNAJB1 bound to ATPγN and ATPγN/PKI. d Bar graph showing the dissociation constants (Kd) calculated from the ITC titration curves of PKI5–24 binding to the apo and ATPγN-bound forms of PKA-CWT and PKA-CDNAJB1 (see also Supplementary Table 2).

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