Figure 1
Modular structure of CNTN4. The protein consists of six N-terminal IgC2 domains and four fibronectin type III (FnIII) domains. Each IgC2 domain is restrained by one disulfide bond (SS) that protects half of the domain (marked by red licorice). The numbers of residues that form each domain have been described in the following way: total number of residues for FnIII modules and split into three parts for IgC2 modules i.e. the number of residues harbored by disulfide bridge (in the square bracket) surrounded by the number of residues before and after disulfide bridge. The length of the protein is ~45 nm, when the domains are aligned. The number of free amino acids (aa) linking each pair of consecutive modules is shown. The first four IgC2 domains preferentially assume a horseshoe conformation.
