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Figure 1.
Figure 1. Overall structure. (a) Structural alignment of the
p38α – β-OG complex (green) and native p38α (gray) using
the coordinate of PDB ID 1P38.^19 The phosphorylation lip of the
native p38 as well as the N′ and C′ lobes are indicated. The
phosphorylation lip of the β-OG complex is not shown due to
local disorder. The overall kinase topology is maintained
although a minor change in the inter-lobe orientation is
apparent. All molecular graphics shown here were rendered using
PyMol [http://pymol.sourceforge.net/]. (b) Ribbon representation
of the p38α – β-OG complex with the two β-OG molecules
shown as spheres. The MAP kinase insert is shown in gray. The
β-OG 1 (carbon atoms shown in orange) is characterized by the
relatively lower B-factor whereas β-OG 2 (carbon atoms shown in
magenta) by higher values (see Table 1). (c) Difference electron
density map (F[obs]–F[calc]) calculated at a 2.0σ cutoff at
the resolution range of 32.7 Å−1.8 Å after the
initial cycle of refinement without β-OG in the model,
superimposed with the final coordinates of the p38α – β-OG
complex. The map clearly indicates the presence of β-OG in site
1.
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