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Fig. 6. (A) Detailed representation of the cis and trans interfaces in the 3D array packing generated with the Dsc2 model using the C-cadherin ectodomain structure (Boggon et al., 2002). Monomers from opposed cell surfaces (yellow and blue) form trans-interactions mediated by Trp2 in the N-terminal domain (EC1' and EC1'' respectively). The Trp side chain is shown binding into the hydrophobic pocket of the opposed N-terminal domain. Cis interactions occur between the EC1' domain (yellow) and the linker region between the EC2 and EC3 domains on another monomer from the same cell surface (red). (B) Zoom view of the linker region. The EC1' domain (yellow) from one monomer inserts the ß-helix region, as a wedge, into the cavity formed between the EC2 and EC3 domains of a neighbouring molecule (red). This cis interface blocks access to the most-exposed calcium-binding site occupied by Ca3. The other two calcium ions, Ca1 and Ca2 are bound deeper into the core of domain EC2. Ca1 and Ca2 are coordinated by five ligand groups from different side chains and two groups from the main chain (not shown). Ca3 is coordinated only by four ligand groups from side chains in EC2 and EC3. The figure was prepared using SETOR.
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