Skip to main content
. 2024 Apr 11;16(4):528. doi: 10.3390/pharmaceutics16040528

Figure 6.

Figure 6

ATP- and substrate-binding sites of Dyrk1A. (A) Close-up view of ADPNP (ATP analogue) bound to the ATP-binding site of Dyrk1A (PDB: 7A4O) [79]. The polar interactions between Dyrk1A and ADPNP (stick representation) are only shown as dashed lines. (B) Close-up view of the interactions of the consensus substrate peptide RARPTPALRE with Dyrk1A (PDB: 2WO6) [98]. Polar interactions are shown as dashed lines. The Dyrk1A interacting residues are in black, whereas the residues of the peptide are in blue italics. The numbering of the peptide residues starts at 0 for the threonine residue which is due to phosphorylation. (C,D) Superposition of small (C) and large (D) ATP-competitive inhibitors with ADPNP as in their crystal structures with Dyrk1A. The adenosine moiety of ADPNP is in yellow and its phosphate groups are in orange. In panel (C), the natural inhibitor harmine is shown in green (PDB: 3ANR) [97] and the VER-239353 inhibitor in cyan (PDB: 7A5N) [79]. In panel (D), the AZ191 inhibitor is shown in light pink (PDB: 8C3G) [101] and the DJM2005 inhibitor (PDB: 2VX3) [98] in deep blue. Images were created with PyMOL 1.8.0.4 version.