Abstract
Teneurins and latrophilins are both conserved families of cell adhesion proteins that mediate cellular communication and play critical roles in embryonic and neural development. However, their mechanisms of action remain poorly understood. In the past several years, three-dimensional structures of teneurins and latrophilins have been reported at atomic resolutions and revealed distinct protein folds and unique structural features. In this review, we discuss these structures which, together with structure-guided biochemical and functional analyses, provide hints for the mechanisms of trans-cellular communication at the synapse and other cell-cell contact sites.