3vkf | pdb_00003vkf

Crystal Structure of Neurexin 1beta/Neuroligin 1 complex

spinqualitylabelsall models 3vkf, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3vkf is a 4 chain structure with sequence from Bos taurus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: BMA, CA, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function NLGN1_RAT Cell surface protein involved in cell-cell-interactions via its interactions with neurexin family members. Plays a role in synapse function and synaptic signal transmission, and probably mediates its effects by recruiting and clustering other synaptic proteins. May promote the initial formation of synapses, but is not essential for this. In vitro, triggers the de novo formation of presynaptic structures. May be involved in specification of excitatory synapses. Publication Abstract from PubMed Polymorphic adhesion molecules neurexin and neuroligin (NL) mediate asymmetric trans-synaptic adhesion, which is crucial for synapse development and function. It is not known whether or how individual synapse function is controlled by the interactions between variants and isoforms of these molecules with differing ectodomain regions. At a physiological concentration of Ca(2+), the ectodomain complex of neurexin-1 beta isoform (Nrx1beta) and NL1 spontaneously assembled into crystals of a lateral sheet-like superstructure topologically compatible with transcellular adhesion. Correlative light-electron microscopy confirmed extracellular sheet formation at the junctions between Nrx1beta- and NL1-expressing non-neuronal cells, mimicking the close, parallel synaptic membrane apposition. The same NL1-expressing cells, however, did not form this higher-order architecture with cells expressing the much longer neurexin-1 alpha isoform, suggesting a functional discrimination mechanism between synaptic contacts made by different isoforms of neurexin variants. Higher-order architecture of cell adhesion mediated by polymorphic synaptic adhesion molecules neurexin and neuroligin.,Tanaka H, Miyazaki N, Matoba K, Nogi T, Iwasaki K, Takagi J Cell Rep. 2012 Jul 26;2(1):101-10. doi: 10.1016/j.celrep.2012.06.009. Epub 2012, Jul 20. PMID:22840401 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Neurexin Neuroligin

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