Figure 2 - full size

 

Figure 2.
Fig. 2. The DFG motif and activation loop adopt different conformations dependent on the bound ligand. (a) Superposition of Nek2-T175A^ATPγS (yellow), Nek2^ADP (orange) and Nek2-T175A^SU (green) protein structures shown as a ribbon in two orientations related by a 90° rotation about the y-axis. (b) Stereoview of Nek2-T175A^ATPγS (yellow carbon atoms) and Nek2^ADP (orange carbon atoms) superposition at the DFG motif. (c) Stereoview of Nek2-T175A^ATPγS (yellow carbon atoms) and Nek2-T175A^SU (green carbon atoms) superposition at the DFG motif. (d) Stereoview of Nek2-T175A^ATPγS (yellow carbon atoms) and Nek2-T175A^Apo (light pink carbon atoms) superposition at the DFG motif. (e) Schematic of the secondary structures adopted by the four Nek2 structures and the amino acid sequence surrounding the DFG motif in Nek2 and Aurora-A. (f) Superposition of three Nek2 conformations of the DFG motif together with the likely position adopted in the fully active conformation based on the Aurora-A/TPX2 structure (magenta). The orientation is that of panels (b) to (d) viewed from the bottom left to the top right.

The above figure is reprinted from an Open Access publication published by Elsevier: J Mol Biol (2009, 386, 476-485) copyright 2009.