Figure 2

MK5 models. A: Final backbone Cα-traces of the MK5 homolog model based on the crystal structure of MK3 (3FHR). The model predicts an N-terminal lobe consisting of a bundle of β-sheets and a conserved α-helix. The C-terminal lobe is largely helical and contains a segment, the activation segment, which includes Thr182 that becomes phosphorylated when MK5 is activated. The hinge region connects the two lobes, and this is where the ATP binding site is predicted to reside. Color coding: Purple via blue, green and yellow to red from N-terminal to C-terminal. B: Final backbone Cα-traces of the MK5 homolog model based on the crystal structure of MK2 (3M2W). Color coding as Figure 2A. C: Final backbone Cα-traces of the MK5 homolog model based on the crystal structure of MK2 (2OZA). Color coding as Figure 2A.