5L2E

Crystal structure of rat Glutamate receptor delta-2 extracellular domain

5L2E の概要

• エントリーDOI: 10.2210/pdb5l2e/pdb
• 分子名称: Glutamate receptor ionotropic, delta-2,Glutamate receptor ionotropic, delta-2 (1 entity in total)
• 機能のキーワード: synapse protein, cell surface protein, glycoprotein, nervous system, protein binding
• 由来する生物種: Rattus norvegicus (Rat); 詳細
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q63226
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 233501.44

構造登録者

Cheng, S.,Ozkan, E. (登録日: 2016-08-01, 公開日: 2016-12-28, 最終更新日: 2024-10-23)

主引用文献

Cheng, S.,Seven, A.B.,Wang, J.,Skiniotis, G.,Ozkan, E.
Conformational Plasticity in the Transsynaptic Neurexin-Cerebellin-Glutamate Receptor Adhesion Complex.
Structure, 24:2163-2173, 2016

PubMed Abstract: Synaptic specificity is a defining property of neural networks. In the cerebellum, synapses between parallel fiber neurons and Purkinje cells are specified by the simultaneous interactions of secreted protein cerebellin with pre-synaptic neurexin and post-synaptic delta-type glutamate receptors (GluD). Here, we determined the crystal structures of the trimeric C1q-like domain of rat cerebellin-1, and the first complete ectodomain of a GluD, rat GluD2. Cerebellin binds to the LNS6 domain of α- and β-neurexin-1 through a high-affinity interaction that involves its highly flexible N-terminal domain. In contrast, we show that the interaction of cerebellin with isolated GluD2 ectodomain is low affinity, which is not simply an outcome of lost avidity when compared with binding with a tetrameric full-length receptor. Rather, high-affinity capture of cerebellin by post-synaptic terminals is likely controlled by long-distance regulation within this transsynaptic complex. Altogether, our results suggest unusual conformational flexibility within all components of the complex.

PubMed: 27926833
DOI: 10.1016/j.str.2016.11.004

実験手法

X-RAY DIFFRACTION (4.152 Å)