Ca2+ and/or Na+ in the central pore (Donegan et al., 2014; Han and Kursula, 2015). Recent findings on the extracellular domain of FLRT3 reveal that this protein has the tendency to homo-dimerize but a precise characterization of dimerization potential is currently unknown. Moreover, the study of FLRT2-LRR, alone and in complex with the cell surface receptor uncoordinated-5 D (UNC5D) revealed that FLRT2-UNC5D interaction controls neuronal radial migration whereas FLRT-FLRT interaction modulates spatial organization in the tangential axis (Seiradake et al., 2014). Subsequently, the same group solved the crystal structure of mouse LPHN3 lectin and olfactomedin-like domains, confirming that the OLF domain is a 5-bladed β-propeller containing a Ca2+ and a Na+ binding sites (Jackson et al., 2015).
