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Figure 1.
FIGURE 1. Crystal structure of the p38  -MK2 heterodimer. A,
side view of the p38 -MK2 heterodimer. P38
(yellow) and MK2
(magenta) are positioned "face to face" in the heterodimer,
which means that the ATP-binding sites and the substrate binding
grooves are at the interface of the heterodimer. The K-helix
of the MK2 C-terminal regulatory domain (blue) is sandwiched
between the p38 and MK2 kinase domains,
whereas residues 370–393 of the C-terminal regulatory domain
bind p38 in the docking groove.
B, heterodimer rotated 180°. C, top view of the heterodimer.
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