3be8
Crystal structure of the synaptic protein neuroligin 4
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OverviewOverview
The neuroligins are postsynaptic cell adhesion proteins whose associations, with presynaptic neurexins participate in synaptogenesis. Mutations in the, neuroligin and neurexin genes appear to be associated with autism and, mental retardation. The crystal structure of a neuroligin reveals features, not found in its catalytically active relatives, such as the fully, hydrophobic interface forming the functional neuroligin dimer; the, conformations of surface loops surrounding the vestigial active center;, the location of determinants that are critical for folding and processing;, and the absence of a macromolecular dipole and presence of an, electronegative, hydrophilic surface for neurexin binding. The structure, of a beta-neurexin-neuroligin complex reveals the precise orientation of, the bound neurexin and, despite a limited resolution, provides substantial, information on the Ca(2+)-dependent interactions network involved in, trans-synaptic neurexin-neuroligin association. These structures exemplify, how an alpha/beta-hydrolase fold varies in surface topography to confer, adhesion properties and provide templates for analyzing abnormal, processing or recognition events associated with autism.
About this StructureAbout this Structure
3BE8 is a Single protein structure of sequence from Homo sapiens with , , , , and as ligands. Known structural/functional Sites: , , , , , , , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Structural Analysis of the Synaptic Protein Neuroligin and Its beta-Neurexin Complex: Determinants for Folding and Cell Adhesion., Fabrichny IP, Leone P, Sulzenbacher G, Comoletti D, Miller MT, Taylor P, Bourne Y, Marchot P, Neuron. 2007 Dec 20;56(6):979-91. PMID:18093521
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