5O5I

Robo1 Ig5

5O5I の概要

• エントリーDOI: 10.2210/pdb5o5i/pdb
• 分子名称: Roundabout homolog 1 (2 entities in total)
• 機能のキーワード: neuronal receptor, signaling protein
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : Q9Y6N7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9813.10

構造登録者

Aleksandrova, N.,Gutsche, I.,Kandiah, E.,Avilov, S.V.,Petoukhov, M.V.,Seiradake, E.,McCarthy, A.A. (登録日: 2017-06-01, 公開日: 2018-01-17, 最終更新日: 2024-11-13)

主引用文献

Aleksandrova, N.,Gutsche, I.,Kandiah, E.,Avilov, S.V.,Petoukhov, M.V.,Seiradake, E.,McCarthy, A.A.
Robo1 Forms a Compact Dimer-of-Dimers Assembly.
Structure, 26:320-328.e4, 2018

PubMed Abstract: Roundabout (Robo) receptors provide an essential repulsive cue in neuronal development following Slit ligand binding. This important signaling pathway can also be hijacked in numerous cancers, making Slit-Robo an attractive therapeutic target. However, little is known about how Slit binding mediates Robo activation. Here we present the crystal structure of Robo1 Ig1-4 and Robo1 Ig5, together with a negative stain electron microscopy reconstruction of the Robo1 ectodomain. These results show how the Robo1 ectodomain is arranged as compact dimers, mainly mediated by the central Ig domains, which can further interact in a "back-to-back" fashion to generate a tetrameric assembly. We also observed no change in Robo1 oligomerization upon interaction with the dimeric Slit2-N ligand using fluorescent imaging. Taken together with previous studies we propose that Slit2-N binding results in a conformational change of Robo1 to trigger cell signaling.

PubMed: 29307485
DOI: 10.1016/j.str.2017.12.003

実験手法

X-RAY DIFFRACTION (3.01 Å)