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Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
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Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
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Journal Article
Structural insights into modulation and selectivity of transsynaptic neurexin–LRRTM interaction
2018
Overview
Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Neurexins (Nrxns) and heparan sulfate proteoglycans have been identified as presynaptic ligands for LRRTMs. Specifically, LRRTM1 and LRRTM2 bind to the Nrxn splice variant lacking an insert at the splice site 4 (S4). Here, we report the crystal structure of the Nrxn1β–LRRTM2 complex at 3.4 Å resolution. The Nrxn1β–LRRTM2 interface involves Ca
2+
-mediated interactions and overlaps with the Nrxn–neuroligin interface. Together with structure-based mutational analyses at the molecular and cellular levels, the present structural analysis unveils the mechanism of selective binding between Nrxn and LRRTM1/2 and its modulation by the S4 insertion of Nrxn.
Leucine-rich repeat transmembrane neuronal proteins (LRRTMs) function as postsynaptic organizers that induce excitatory synapses. Here authors solve the crystal structure of LRRTM2 in complex with its ligand Nrxn1β and shed light on how selective binding of ligands to LRRTM1/2 is achieved.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 14/19
/ 82/103
/ 82/80
/ 82/83
/ Animals
/ Calcium
/ Cell Adhesion Molecules, Neuronal - chemistry
/ Cell Adhesion Molecules, Neuronal - metabolism
/ Heparan sulfate proteoglycans
/ Humanities and Social Sciences
/ Humans
/ Leucine
/ Membrane Proteins - chemistry
/ Membrane Proteins - metabolism
/ Mice
/ Mutant Proteins - metabolism
/ Nerve Tissue Proteins - chemistry
/ Nerve Tissue Proteins - metabolism
/ Neural Cell Adhesion Molecules - chemistry
/ Neural Cell Adhesion Molecules - metabolism
/ Proteins
/ Science
/ Synapses
