3BE8

Crystal structure of the synaptic protein neuroligin 4

Summary for 3BE8

• Entry DOI: 10.2210/pdb3be8/pdb
• Descriptor: Neuroligin-4, X-linked, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRATE ANION, ... (8 entities in total)
• Functional Keywords: neuroligin, cell adhesion protein, synaptic protein, a/b-hydrolase fold, four-helix bundle, glycoprotein, membrane, transmembrane, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Single-pass type I membrane protein (Potential): Q8N0W4
• Total number of polymer chains: 2
• Total formula weight: 134333.28

Authors

Fabrichny, I.P.,Leone, P.,Sulzenbacher, G.,Comoletti, D.,Miller, M.T.,Taylor, P.,Bourne, Y.,Marchot, P. (deposition date: 2007-11-16, release date: 2008-01-29, Last modification date: 2024-11-20)

Primary citation

Fabrichny, I.P.,Leone, P.,Sulzenbacher, G.,Comoletti, D.,Miller, M.T.,Taylor, P.,Bourne, Y.,Marchot, P.
Structural Analysis of the Synaptic Protein Neuroligin and Its beta-Neurexin Complex: Determinants for Folding and Cell Adhesion
Neuron, 56:979-991, 2007

PubMed Abstract: 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 Ca2+-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.

PubMed: 18093521
DOI: 10.1016/j.neuron.2007.11.013

Experimental method

X-RAY DIFFRACTION (2.2 Å)