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Figure 5


Fig. 5. Kinetics analyses of the association of GST-WW2 of Nedd4 with the phosphorylated and non-phosphorylated extended PY motif of Cx43. (A) Plot of steady-state binding of Cx43 CTphosph ({circ}) and Cx43 CT ({blacksquare}) against GST-WW2 concentration. The lines represent the best fit to the equation RU=RUmax/(1+KDapp/S). RU and RUmax are the resonance and the maximal resonance of bound GST-WW2, S is its free concentration, and KDapp is the apparent equilibrium dissociation constant. KDapp values (in µM) are listed as means ± s.e.m. in the table. NB, no binding. (B) GST-WW2 fusion protein (0.39 µM) was pre-incubated with increasing concentrations of non-biotinylated Cx43 CTphosph peptide, and the mixture was applied to a sensor chip with immobilized Cx43 CTphosph peptide at its surface. The steady-state signal B was expressed as B/Bmax, where Bmax is the steady-state signal at zero competing peptide. Binding of GST-WW2 to the immobilized Cx43 CTphosph decreased with increasing amounts of competing peptides.





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