Figure 1.

A) Sequence alignment of the 16 terminal amino acids of VE-Cadherin. Position indicates the register of amino acids relative to the c-terminal denoted as 0. The mouse (M. musculus) sequence shown corresponds to the exact peptide used in NMR titration studies, with numbers above corresponding to amino acid location in primary sequence. Conserved acidic residues are shown in red, and potential phosphorylation sites are depicted in green. B) Chemical shift perturbations induced by VE-Cad peptide binding mapped onto the structure of ligand free par3-PDZ3. Differences in amide chemical shifts were defined as: Δδ_ppm = [(5*Δδ_HN)² + (Δδ_N)²]^1/2, where Δδ_HN and Δδ_N represent chemical shift differences of the free and bound forms of par3-PDZ3. Oval highlight represents location of the binding groove between the β2-strand and the α2-helix, site of canonical c-terminal ligand binding. Positions of basic patch residues (K⁶⁰⁶, R⁶⁰⁹, K⁶¹¹, K⁶²²) located in the β2 and β3-strands are shown to distinguish areas of distal ligand binding.