3BE8

Crystal structure of the synaptic protein neuroligin 4

3BE8 の概要

• エントリーDOI: 10.2210/pdb3be8/pdb
• 分子名称: Neuroligin-4, X-linked, 2-acetamido-2-deoxy-beta-D-glucopyranose, CITRATE ANION, ... (8 entities in total)
• 機能のキーワード: neuroligin, cell adhesion protein, synaptic protein, a/b-hydrolase fold, four-helix bundle, glycoprotein, membrane, transmembrane, cell adhesion
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): Q8N0W4
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 134333.28

構造登録者

Fabrichny, I.P.,Leone, P.,Sulzenbacher, G.,Comoletti, D.,Miller, M.T.,Taylor, P.,Bourne, Y.,Marchot, P. (登録日: 2007-11-16, 公開日: 2008-01-29, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.2 Å)