Fig. 3. Conserved tyrosines in the cytoplasmic domain of VEC. (A) Sequence alignment of cytoplasmic domains of VEC from mouse, rat, human and chicken, and mouse E-cadherin. Tyrosines conserved in VEC and their relative position (mouse versus human) are indicated in green. Identical residues, conserved and semi-conserved substitutions are indicated by asterisks, colons and dots, respectively. Grey boxes correspond to those parts of E-cadherin that interact with β-catenin when crystallized together (Huber and Weis, 2001). (B) Mouse VEC was computer-modeled on the crystal structure of mouse E-cadherin in the E-cadherin–β-catenin complex (i.e. boxed in A) (pdb: 1i7x, 1i7w). Shown in the left panel is a ribbon representation of this model with the position and orientation of six tyrosines highlighted in green. The right panels represent enlarged views of areas surrounding these tyrosines. The β-catenin chain is in a space filling representation. Significantly, in this model, Y685, the residue predominantly phosphorylated following VEGF stimulation (Wallez et al., 2006), is not accessible when β-catenin is bound.