Figure 3 - full size

 

Figure 3.
Figure 3 NMR spectral perturbation study of various activation states of EphB2 kinase. (A) Overlay of a representative region of the ^1H,^15N-HSQC spectra of the auto-inhibited EphB2 JMS-KD fragment (black) and the activated EphB2 KD fragment (blue). (B) Residues experiencing spectral perturbations are mapped onto the structure of the EphB2 JMS-KD as relative peak intensities with a linear gradient from white (I/I[ref] than or equal to 0.4) to blue (I/I[ref]=0). Spheres represent the nitrogen atoms of affected residues. (C) As panel A, but for the EphB2 JMS-KD fragment phosphorylated on residues Y604 and Y610 (red). (D) As panel B, but for the phospho-JMS-KD fragment using a linear gradient from white to red. (E) As panel A, but for the EphB2 Y750A JMS-KD mutant (green). (F) As panel B, but for the EphB2 Y750A JMS-KD mutant using a linear gradient from white to green. In all spectral overlays, residues exhibiting significant spectral perturbations are labeled. JMS residues are underlined, whereas residues in the activation segment are in italics. Dotted lines indicate large chemical shift changes between the phosphorylated and unphosphorylated EphB2 JMS-KD fragment, whereas arrows highlight the positions of peaks appearing around 8.0 p.p.m. in the spectrum of the phosphorylated EphB2 JMS-KD.

The above figure is reprinted by permission from Macmillan Publishers Ltd: EMBO J (2006, 25, 4686-4696) copyright 2006.