6FAY

Teneurin3 monomer

6FAY の概要

• エントリーDOI: 10.2210/pdb6fay/pdb
• EMDBエントリー: 4219
• 分子名称: Odz3 protein, 2-acetamido-2-deoxy-beta-D-glucopyranose (2 entities in total)
• 機能のキーワード: neuronal cell adhesion, bacterial toxin-like, cell adhesion
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 212535.77

構造登録者

Janssen, B.J.C.,Meijer, D.H.M.,van Bezouwen, L.S. (登録日: 2017-12-18, 公開日: 2018-03-28, 最終更新日: 2024-10-23)

主引用文献

Jackson, V.A.,Meijer, D.H.,Carrasquero, M.,van Bezouwen, L.S.,Lowe, E.D.,Kleanthous, C.,Janssen, B.J.C.,Seiradake, E.
Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction.
Nat Commun, 9:1079-1079, 2018

PubMed Abstract: Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.

PubMed: 29540701
DOI: 10.1038/s41467-018-03460-0

実験手法

ELECTRON MICROSCOPY (3.8 Å)