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4V2A

human Unc5A ectodomain

4V2A の概要
エントリーDOI10.2210/pdb4v2a/pdb
関連するPDBエントリー4V2B 4V2C 4V2D 4V2E
分子名称NETRIN RECEPTOR UNC5A, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
機能のキーワードapoptosis, uncoordinated-5, unc5a, netrin receptor, flrt
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33782.22
構造登録者
主引用文献Seiradake, E.,Del Toro, D.,Nagel, D.,Cop, F.,Haertl, R.,Ruff, T.,Seyit-Bremer, G.,Harlos, K.,Border, E.C.,Acker-Palmer, A.,Jones, E.Y.,Klein, R.
Flrt Structure: Balancing Repulsion and Cell Adhesion in Cortical and Vascular Development
Neuron, 84:370-, 2014
Cited by
PubMed Abstract: FLRTs are broadly expressed proteins with the unique property of acting as homophilic cell adhesion molecules and as heterophilic repulsive ligands of Unc5/Netrin receptors. How these functions direct cell behavior and the molecular mechanisms involved remain largely unclear. Here we use X-ray crystallography to reveal the distinct structural bases for FLRT-mediated cell adhesion and repulsion in neurons. We apply this knowledge to elucidate FLRT functions during cortical development. We show that FLRTs regulate both the radial migration of pyramidal neurons, as well as their tangential spread. Mechanistically, radial migration is controlled by repulsive FLRT2-Unc5D interactions, while spatial organization in the tangential axis involves adhesive FLRT-FLRT interactions. Further, we show that the fundamental mechanisms of FLRT adhesion and repulsion are conserved between neurons and vascular endothelial cells. Our results reveal FLRTs as powerful guidance factors with structurally encoded repulsive and adhesive surfaces.
PubMed: 25374360
DOI: 10.1016/J.NEURON.2014.10.008
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.4 Å)
構造検証レポート
Validation report summary of 4v2a
検証レポート(詳細版)ダウンロードをダウンロード

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件を2024-10-30に公開中

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