2vh8

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spinqualitylabelsall models 2vh8, resolution 3.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF SYNAPTIC PROTEIN NEUROLIGIN 4 IN COMPLEX WITH NEUREXIN BETA 1.

Overview

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 Structure

2VH8 is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Wed Jan 23 11:04:28 2008