4V2A
human Unc5A ectodomain
4V2A の概要
エントリーDOI | 10.2210/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 | 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. (登録日: 2014-10-08, 公開日: 2014-11-05, 最終更新日: 2020-07-29) |
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: 25374360DOI: 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) |
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