5z8y | pdb_00005z8y

Crystal structure of human LRRTM2 in complex with Neurexin 1beta

spinqualitylabelsall models 5z8y, resolution 3.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5z8y is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.4Å Ligands: CA, FUC, NAG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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). Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neurexin

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