Title : Nectin ectodomain structures reveal a canonical adhesive interface
Abstract :
- Nectins are immunoglobulin superfamily glycoproteins that mediate intercellular adhesion in many vertebrate tissues
- Homophilic and heterophilic interactions between nectin family members help mediate tissue patterning
- We determined the homophilic binding affinities and heterophilic specificities of all four nectins and the related protein nectin-like 5 (Necl-5 ) from human and mouse, revealing a range of homophilic interaction strengths and a defined heterophilic specificity pattern
- To understand the molecular basis of their adhesion and specificity, we determined the crystal structures of natively glycosylated full ectodomains or adhesive fragments of all four nectins and Necl-5
- All of the crystal structures revealed dimeric nectins bound through a stereotyped interface that was previously proposed to represent a cis dimer
- However, conservation of this interface and the results of targeted cross-linking experiments showed that this dimer probably represents the adhesive trans interaction
- The structure of the dimer provides a simple molecular explanation for the adhesive binding specificity of nectins