Figure 4 - full size



	Figure 4 - full size

Figure 4.
Figure 4 ATP binding and DFG/D pockets. Stereo diagrams depicting details of the ATP and DFG/D pockets. Critical residues are labeled. Hydrogen bonds and ionic interactions are depicted by dashed lines. (A) Mnk1-KR with an ionic interaction network involving the Asp residues of the DFD motif. The conserved Lys–Glu ion pair is broken. The final 2F[o]-F[c] electron density (gray; contoured at the 1 level) is shown covering selected residues. (B) Mnk2-KR (Jauch et al, 2005) (PDB-ID 2AC3) in which the DFD-out conformation is retained, although the activation segment has been detached from the N-terminal lobe. No clear interaction involving the Asp residues of the DFD motif can be discerned. (C) DAPK1-Mn^2+–AMPPNP complex (Tereshko et al, 2001) (PDB ID 1IG1). The AMPPNP is shown in ball-and-stick (carbon—brown; phosphorus—pink; Mn^2+—black sphere; water—blue spheres). (D) Mnk2–KR^D228G–staurosporine complex. Staurosporine is shown in ball-and-stick (carbon—brown). Note the complete reversal of the DFD-out to the DFD-in conformation upon staurosporine binding (compare to panel B). The final 2F[o]–F[c] electron density (gray; contoured at the 1 level) is shown covering staurosporine and selected residues.