Fig. 1 A single amino acid difference in the ATP-binding domain of GSK3α and GSK3β results in structural and topological differences. A single amino acid.

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Fig. 1 A single amino acid difference in the ATP-binding domain of GSK3α and GSK3β results in structural and topological differences. A single amino acid difference in the ATP-binding domain of GSK3α and GSK3β results in structural and topological differences. (A) Aligned primary amino acid sequences of GSK3α and GSK3β. Residue differences between the two paralogs are in red. The main regions of the kinases are color-coded: hinge (yellow), backend region (green), P-loop (pink), DFG motif (blue), and activation loop (orange). Key amino acids for autoregulation, S21/9 and Y279/216, are underlined. Amino acids within 6 Å of the ligand are marked by an asterisk. (B) X-ray crystal structure (2.4 Å resolution) of hGSK3β bound to BRD0209, a dual GSK3α/β inhibitor. The inset shows a hydrogen bond network centered on the Asp133 side chain, on the backend region of the hinge connecting the N- and C-lobes of GSK3. The main regions of the kinases are again color-coded. (C) A comparison between the hinge backend and ATP-binding site of apo GSK3β and an MD simulation of apo GSK3α highlight the size difference between their hydrophobic pockets. Florence F. Wagner et al., Sci Transl Med 2018;10:eaam8460 Published by AAAS