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Figure 3.
Figure 3. Structural characteristics of β-OG binding to
p38α. (a) Superimposition of the p38α – β-OG complex
(green) and native p38α (gray) in the vicinity of the MAP
kinase insert. The β-OG molecules are represented as spheres in
orange and magenta for β-OG 1 and 2, respectively. Trp197 and
Met198 from the αEF/αF loop of native p38α and the p38α –
β-OG complex are shown as sticks. The MAP kinase insert goes
through a conformational change and opens up to accommodate the
β-OG molecule. In addition the αEF/αF loop including Trp197
and Met198 goes through a substantial conformational change. In
this context, Trp197 forms a hydrophobic interaction with the
aliphatic segment of the detergent molecule. (b) Surface
representation of p38α displaying the shape of the lipid
binding site that accommodates β-OG 1 (orange) and β-OG 2
(magenta). β-OG 1 is extensively buried in the binding site
whereas only the lipid tail of β-OG 2 interacts with the
protein. The MAP kinase insert is highlighted in a darker
surface colour.
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