Fig. 1
Binding specificity of paxillin LD motifs for FAK and vinculin. (A) Schematic domain structures of FAK, paxillin and vinculin. Residue numbers of domain boundaries are indicated; for LD motifs starting residue numbers for LD1, LD2 and LD4 are shown. (B) Binding curves for FITC labelled paxillin LD peptides to the FAT domain of FAK were determined by fluorescence anisotropy. LD2/4 contains sequences of LD2 and LD4 separated by a linker (see Tab.S1). (C) Binding curves for FITC labelled paxillin LD peptides to full-length vinculin (Vin-FL). (D) Binding curves for FITC labelled paxillin LD peptides to the vinculin tail domain (Vin-T). (B-C) Apparent KD values are obtained from fitting a one-site binding model. Resulting KD values with an error > 25% are considered not determined (ND). Error bars represent SD from 4 measurements