Supplementary Figure 3: Changes in 1H-15N TROSY spectra of p38α upon dual phosphorylation. | Nature Structural & Molecular Biology

Supplementary Figure 3: Changes in 1H-15N TROSY spectra of p38α upon dual phosphorylation.

From: Allosteric enhancement of MAP kinase p38α's activity and substrate selectivity by docking interactions

Supplementary Figure 3

Comparison of 1H-15N TROSY spectra of unphosphorylated p38α (p38α-0P; black) and p38α-2P (red) in the absence of ATP. The regions containing the resonances of Met179, Thr180, Gly181, Tyr182, and Val183, which are located in the activation loop, are expanded to indicate that these resonances disappeared upon dual phosphorylation. In the lower left panel, the signal from p38α-2P, which overlaps with the Met179 signal from p38α-0P, does not belong to Met179 and is presumably from the unassigned resonance (n.a.) below.

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