Review Article

Exploring the Nature of Desmosomal Cadherin Associations in 3D

Figure 3

A visual representation of alternative desmosomal cadherin association models from the strand dimer (a), that consider the heterophilic interactions of desmosomal cadherins. Individual desmosomal cadherin ectodomains (1 to 5) are portrayed as ovals and are colored accordingly to clearly separate lateral from strand interactions. Identical color-coding is used to separate lateral and strand interactions in the ribbon representations. Cadherin ectodomains spanning from one cell surface are colored dark or light blue respectively and ectodomains spanning from an opposing cell surface are shown in green. (b) Cadherin dimerization via the surface of EC1 domains containing residues (residues not shown). Lateral dimers interact with strand dimers from an opposing cell. The insert shows a ribbon representation of the Trp2-mediated lateral-contact. (c) Lateral dimerization via EC1/EC2 calcium binding sites facilitated by the rod-like shape of cadherin ectodomains. The inset shows a ribbon representation of the domain pair dimer from the same cell surface, the position of the calcium ions are represented by spheres and are color coded dark or light blue to represent the cadherin ectodomains in c. (d) Lateral interaction at EC1 between strand dimers bound together by EC1 and EC2 interactions. The left inset is a ribbon representation of Trp2 mediated contact between N-terminal domains; the right inset is a ribbon representation of lateral interactions between EC1 and EC2 domains. (e) Adhesive interactions between antiparallel cadherin molecules along their full length. Strand interactions occur between more than two EC domains resulting in the formation of three types of adhesive complexes of different length. Modified from [53] with permission from Birkhäuser Verlag AG.
930401.fig.003a
(a)
930401.fig.003b
(b)
930401.fig.003c
(c)
930401.fig.003d
(d)
930401.fig.003e
(e)