Structure
Neuroligins bind with the aid of Ca2+ to the α-neurexin LNS (laminin, neurexin and sex hormone-binding globulin-like folding units) domains and to the β-neurexin LNS domain which then establishes a heterophilic trans-synaptic recognition code. Through the observation of the crystal structure of neuroligin-1, it was determined that neuroligin-1 forms a dimer when two neurexin-1 beta monomers bind to the neuroligin-1’s two opposite surfaces. This forms a heterotetramer, which contains an interface for binding Ca2+. The interaction of neuroligin and neurexin to form a heterotetramer is monitored by alternatively spliced sites located near the binding interface for Ca2+ in both the neuroligin-1 and the neurexin-1 beta.
The extracellular domain of NLGN consists mostly of a region that is homologous to acetylcholinesterases, but the amino acids important for catalysis in AChE are not conserved in NLGN, which lack esterase activity. Furthermore, this AChE homologous region is crucial for the proper function of NLGN.
Read more about this topic: Neuroligin
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