journal menu
![[Figure 9]](cb5088fig9mag.jpg)
|
|
Figure 9
Comparison of the ERK5 allosteric ligand-binding mode with allosteric inhibitors of (a, b) MEK1/2 (PDB entries 1s9i and 1s9j; Ohren et al., 2004  ), (c) ITK (PDB entry 4m0y; Han et al., 2014) and (d) CDK2 (PDB entry 3py1; Betzi et al., 2011) highlights the changes in αC helix orientation and P-loop conformation associated with inhibitor binding. In (a), (c) and (d) the structures are oriented such that the viewer looks onto the kinase C-lobe, and the N-terminal β-sheet has been omitted for clarity. In (b) the view has been rotated 90° with respect to (a) to show the differences in P-loop conformation. Structures were superposed by matching residues corresponding to the β-sheet and hinge region of the N-terminal lobe of ERK5 kinase (amino acids 55–61, 70–88, 108–123 and 131–140). ERK5 (coloured as in Fig. 2), MEK (gold), ITK (cyan) and CDK2 (lilac) are shown in ribbon representation. Bound ligands are rendered as sticks with C atoms coloured green (compound 4), pink (ATP), cyan (MEK inhibitor; compound 7), magenta (ITK inhibitor; compound 8), purple (SU9516) and cyan (ANS; compound 9). |
![[Figure 9]](cb5088fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
