The bb′ domains contain a CNX binding site, which is composed of positively charged, highly conserved residues (K214, K274, and R282) that interact with the negatively charged residues of the CNX P domain.
The bb′ regions harbor a CNX interaction site, featuring positively charged, highly preserved amino acid residues (K214, K274, and R282) that interact with the negatively charged components of the CNX P domain.