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. 2017 Apr 7;3(4):e1600663. doi: 10.1126/sciadv.1600663

Fig. 3. Changes of the fast conformational dynamics of the hydrophobic core upon nucleotide and pseudosubstrate binding.

Fig. 3

(A) Order parameters of the methyl groups mapped onto the apo, binary (ATPγC-bound), and ternary (ATPγN/PKI5–24) forms of the enzyme, showing an increasing rigidification of the hydrophobic core. (B) Ordering of the C-spine, αF, and the catalytic loop upon nucleotide and PKI binding. (C). Structural details of PKA-C showing the C-spine and the αE helix, highlighting the rigidification of I150, I180, and V182 upon ligand binding and bridging β1-β2 in the N-lobe with β7-β8 in the C-lobe.