2XB6

Revisited crystal structure of Neurexin1beta-Neuroligin4 complex

2XB6 の概要

• エントリーDOI: 10.2210/pdb2xb6/pdb
• 関連するPDBエントリー: 1C4R 2VH8 2WQZ
• 分子名称: NEUROLIGIN-4, X-LINKED, NEUREXIN-1-BETA, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• 機能のキーワード: alpha-beta-hydrolase fold, autism, conformational rearrangement, cell adhesion
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 174395.36

構造登録者

Leone, P.,Comoletti, D.,Ferracci, G.,Conrod, S.,Garcia, S.U.,Taylor, P.,Bourne, Y.,Marchot, P. (登録日: 2010-04-07, 公開日: 2010-06-23, 最終更新日: 2024-11-13)

主引用文献

Leone, P.,Comoletti, D.,Ferracci, G.,Conrod, S.,Garcia, S.U.,Taylor, P.,Bourne, Y.,Marchot, P.
Structural Insights Into the Exquisite Selectivity of Neurexin-Neuroligin Synaptic Interactions
Embo J., 29:2461-, 2010

PubMed Abstract: The extracellular domains of neuroligins and neurexins interact through Ca(2+) to form flexible trans-synaptic associations characterized by selectivity for neuroligin or neurexin subtypes. This heterophilic interaction, essential for synaptic maturation and differentiation, is regulated by gene selection, alternative mRNA splicing and post-translational modifications. A new, 2.6 A-resolution crystal structure of a soluble neurexin-1beta-neuroligin-4 (Nrx1beta-NL4) complex permits a detailed description of the Ca(2+)-coordinated interface and unveils concerted positional rearrangements of several residues of NL4, not observed in neuroligin-1, associated with Nrx1beta binding. Surface plasmon resonance analysis of the binding of structure-guided Nrx1beta mutants towards NL4 and neuroligin-1 shows that flexibility of the Nrx1beta-binding site in NL4 is reflected in a greater dissociation constant of the complex and higher sensitivity to ionic strength and pH variations. Analysis of neuroligin mutants points to critical functions for two respective residues in neuroligin-1 and neuroligin-2 in governing the affinity of the complexes. Although neuroligin-1 and neuroligin-2 have pre-determined conformations that respectively promote and prevent Nrx1beta association, unique conformational reshaping of the NL4 surface is required to permit Nrx1beta association.

PubMed: 20543817
DOI: 10.1038/EMBOJ.2010.123

実験手法

X-RAY DIFFRACTION (2.6 Å)