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. Author manuscript; available in PMC: 2016 Jul 14.
Published in final edited form as: Biochemistry. 2015 Jul 13;54(28):4307–4319. doi: 10.1021/acs.biochem.5b00506

Figure 6.

Figure 6

Binding of AMP-PNP to inactive and active ERK2. (a) A portion of the Leu/Val region of the 2D HMQC spectra of 0P- and 2P-ERK2 upon titration with AMP-PNP. These spectra show that one of the methyl resonances of L26 is in slow exchange on the NMR chemical shift time scale between free and bound forms for both 0P-and 2P-ERK2. The arrows point to the peak in the free form of ERK2, and the dashed lines outline the position of the free peak. (b) The CSPC,H for methyls between the free and AMP-PNP-bound form is mapped onto the X-ray structure of 0P-ERK2 bound to ATP (PDB 4GT3). The color scale for the CSPC,H values is on the right, with blue indicating no measurable perturbation, red indicating the largest perturbations, and black indicating that these peaks were not observed in the spectra with saturated AMP-PNP, possibly due to chemical exchange broadening in the bound state. The ligand ATP is highlighted with orange sticks. The side chains of the eight catalytic spine residues were shown in magenta sticks. Six out of the eight these residues were I/L/V, with their methyls highlighted with magenta circles.