Figure 2 - full size

 

Figure 2.
Figure 2. Interaction between the mDvl1 PDZ Domain and Fz7(A) ^15N-HSQC spectra of free Fz7 peptide and Fz7 peptide bound to the PDZ domain of mDvl1. The red contour lines represent spectra of the free form of the PDZ domain when no Fz7 peptide (GKTLQSWRRFYH) was present, the green lines (upper inset) represent spectra of partially bound forms of the PDZ domain when 0.86 mM Fz7 peptide was present, and the blue lines represent spectra of the fully bound forms of the PDZ domain when 10 mM Fz7 peptide was present. The concentration of the PDZ domain was 1.1 mM. The two insets show the enlarged regions where the chemical-shift perturbations were small (lower inset) and large (upper inset). In the upper inset, the signals from the same residue but in different spectra were placed in smaller boxes.(B) The figure shows the worm representation of the backbone structure of the mDvl1 PDZ domain. The thickness of the worm is proportional to the weighted sum (in Hz) of the ^1H and ^15N shifts upon binding by the Fz7 peptide (see A), and the increasing chemical-shift perturbation is shown (blue, low; red, high).(C) Ribbon diagram of the PDZ domain structure. The binding site of the Fz7 peptide identified from the chemical-shift perturbation studies is indicated.

The above figure is reprinted by permission from Cell Press: Mol Cell (2003, 12, 1251-1260) copyright 2003.