5z8y
From Proteopedia
Crystal structure of human LRRTM2 in complex with Neurexin 1beta
Structural highlights
Disease[NRX1B_HUMAN] Pitt-Hopkins-like syndrome;Autism;Schizophrenia. Function[LRRT2_HUMAN] Involved in the development and maintenance of excitatory synapse in the vertebrate nervous system. Regulates surface expression of AMPA receptors and instructs the development of functional glutamate release sites. Acts as a ligand for the presynaptic receptors NRXN1-A and NRXN1-B (By similarity). [NRX1B_HUMAN] Neuronal cell surface protein that may be involved in cell recognition and cell adhesion by forming intracellular junctions through binding to neuroligins. May play a role in formation or maintenance of synaptic junctions. May mediate intracellular signaling. May play a role in angiogenesis (By similarity). Publication Abstract from PubMedLeucine-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 Nrxn1beta-LRRTM2 complex at 3.4 A resolution. The Nrxn1beta-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. Structural insights into modulation and selectivity of transsynaptic neurexin-LRRTM interaction.,Yamagata A, Goto-Ito S, Sato Y, Shiroshima T, Maeda A, Watanabe M, Saitoh T, Maenaka K, Terada T, Yoshida T, Uemura T, Fukai S Nat Commun. 2018 Sep 27;9(1):3964. doi: 10.1038/s41467-018-06333-8. PMID:30262834[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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