3B3Q

Crystal structure of a synaptic adhesion complex

3B3Q の概要

• エントリーDOI: 10.2210/pdb3b3q/pdb
• 分子名称: Nlgn1 protein, NRXN1 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: synaptic formation, adhesion, heterophilic, protein-protein complex, calcium binding, membrane, transmembrane, cell adhesion
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 173737.17

構造登録者

Chen, X.,Liu, H.,Shim, A.,Focia, P.,He, X. (登録日: 2007-10-22, 公開日: 2008-01-15, 最終更新日: 2024-10-09)

主引用文献

Chen, X.,Liu, H.,Shim, A.H.,Focia, P.J.,He, X.
Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions.
Nat.Struct.Mol.Biol., 15:50-56, 2008

PubMed Abstract: The heterophilic synaptic adhesion molecules neuroligins and neurexins are essential for establishing and maintaining neuronal circuits by modulating the formation and maturation of synapses. The neuroligin-neurexin adhesion is Ca2+-dependent and regulated by alternative splicing. We report a structure of the complex at a resolution of 2.4 A between the mouse neuroligin-1 (NL1) cholinesterase-like domain and the mouse neurexin-1beta (NX1beta) LNS (laminin, neurexin and sex hormone-binding globulin-like) domain. The structure revealed a delicate neuroligin-neurexin assembly mediated by a hydrophilic, Ca2+-mediated and solvent-supplemented interface, rendering it capable of being modulated by alternative splicing and other regulatory factors. Thermodynamic data supported a mechanism wherein splicing site B of NL1 acts by modulating a salt bridge at the edge of the NL1-NX1beta interface. Mapping neuroligin mutations implicated in autism indicated that most such mutations are structurally destabilizing, supporting deficient neuroligin biosynthesis and processing as a common cause for this brain disorder.

PubMed: 18084303
DOI: 10.1038/nsmb1350

実験手法

X-RAY DIFFRACTION (2.4 Å)