Fig. 5: Comparison of known modes of kinase dimerization and allostery. | Nature Communications

Fig. 5: Comparison of known modes of kinase dimerization and allostery.

From: Granulovirus PK-1 kinase activity relies on a side-to-side dimerization mode centered on the regulatory αC helix

Fig. 5

a Parallel side-to-side homodimer PK-1 (PDB 6VVZ; solved in this study); b allosteric regulation of CDK2 via N-lobe binding to Cyclin (PDB 2CJM)77; c transverse side-to-side homodimer CRAF (PDB 3OMV)38; d back-to-back homodimer IRE1 (PDB 2RIO)41; e head-to-head homodimer IRAK3 (PDB 6RUU)40; f head-to-tail heterodimer EGFR:HER3 (PDB 4RIW)42. Each allosteric or dimerization mode is illustrated by molecular surface (top panel), cartoon ribbon (middle panel) and schematic representation (lower panel). Protomer A and B are coloured tan and grey, respectively. The αC-helix (αC) from protomer A and B are highlighted in dark blue and pink, respectively. The N-lobe (N) and C-lobe (C) are shown, and the KEN domain that contributes to the IRE1 dimer interface is indicated in d.

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