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. Author manuscript; available in PMC: 2020 Jun 1.
Published in final edited form as: IUBMB Life. 2019 May 7;71(6):685–696. doi: 10.1002/iub.2057

FIG 8.

FIG 8

Community map of PKA explored in the context of a distal Y204A mutation. The mutation about 8 Å away from the active site debilitates the kinetics of the kinase. Comparison of the community maps of the mutant and the wild-type PKA allow for understanding the dynamic allostery-based modulations that effect kinase activity. As shown in the active-site cleft, the distal Y204A mutation alters the distribution of the dynamics of the protein and reorganizes its community map. As a result, the mutant is unable to synchronize the nucleotide and peptide substrates optimally at the active site.