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. Author manuscript; available in PMC: 2008 Dec 29.
Published in final edited form as: Chem Biol Drug Des. 2006 Mar;67(3):230–237. doi: 10.1111/j.1747-0285.2006.00361.x

Figure 1. PtdIns(4,5)P2 caused significant chemical shift changes upon binding to the Abl SH2 domain.

Figure 1

15N-edited HSQC spectra of Abl SH2 domain were recorded in the presence of 135 mM KCl, and increasing concentrations of PtdIns(4,5)P2. (A) The spectra were overlaid to show the chemical shift perturbations of NH peaks due to C4-PtdIns(4,5)P2 binding; several including the G14 peak are folded. (B) The chemical shift changes in each residues’ signals at 0.8 mM ligand concentrations were plotted into histograms, with secondary structure taken from PDB 1OPK. The residues exhibiting significant PtdIns(4,5)P2-induced perturbations are shown on the ribbon (C) and molecular surface (D) in red, orange, and yellow indicating large (>10.0), medium (6.0-10.0) and small (2.0-6.0) normalized amide chemical shift changes, respectively.