5KC5

Crystal structure of the Cbln1 C1q domain trimer

5KC5 の概要

• エントリーDOI: 10.2210/pdb5kc5/pdb
• 分子名称: Cerebellin-1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: cerebellin, c1q, neurotransmission, signaling protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16864.03

構造登録者

Elegheert, J.,Clay, J.E.,Siebold, C.,Aricescu, A.R. (登録日: 2016-06-05, 公開日: 2016-07-27, 最終更新日: 2024-10-16)

主引用文献

Elegheert, J.,Kakegawa, W.,Clay, J.E.,Shanks, N.F.,Behiels, E.,Matsuda, K.,Kohda, K.,Miura, E.,Rossmann, M.,Mitakidis, N.,Motohashi, J.,Chang, V.T.,Siebold, C.,Greger, I.H.,Nakagawa, T.,Yuzaki, M.,Aricescu, A.R.
Structural basis for integration of GluD receptors within synaptic organizer complexes.
Science, 353:295-299, 2016

PubMed Abstract: Ionotropic glutamate receptor (iGluR) family members are integrated into supramolecular complexes that modulate their location and function at excitatory synapses. However, a lack of structural information beyond isolated receptors or fragments thereof currently limits the mechanistic understanding of physiological iGluR signaling. Here, we report structural and functional analyses of the prototypical molecular bridge linking postsynaptic iGluR δ2 (GluD2) and presynaptic β-neurexin 1 (β-NRX1) via Cbln1, a C1q-like synaptic organizer. We show how Cbln1 hexamers "anchor" GluD2 amino-terminal domain dimers to monomeric β-NRX1. This arrangement promotes synaptogenesis and is essential for D: -serine-dependent GluD2 signaling in vivo, which underlies long-term depression of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses and motor coordination in developing mice. These results lead to a model where protein and small-molecule ligands synergistically control synaptic iGluR function.

PubMed: 27418511
DOI: 10.1126/science.aae0104

実験手法

X-RAY DIFFRACTION (2.351 Å)