4MT7
Crystal structure of collybistin I
4MT7 の概要
| エントリーDOI | 10.2210/pdb4mt7/pdb |
| 関連するPDBエントリー | 4MT6 |
| 分子名称 | Rho guanine nucleotide exchange factor 9 (1 entity in total) |
| 機能のキーワード | extended conformation, protein binding |
| 由来する生物種 | Rattus norvegicus (rat) |
| 細胞内の位置 | Cytoplasm: Q9QX73 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 57368.11 |
| 構造登録者 | |
| 主引用文献 | Soykan, T.,Schneeberger, D.,Tria, G.,Buechner, C.,Bader, N.,Svergun, D.,Tessmer, I.,Poulopoulos, A.,Papadopoulos, T.,Varoqueaux, F.,Schindelin, H.,Brose, N. A conformational switch in collybistin determines the differentiation of inhibitory postsynapses. Embo J., 33:2113-2133, 2014 Cited by PubMed Abstract: The formation of neuronal synapses and the dynamic regulation of their efficacy depend on the assembly of the postsynaptic neurotransmitter receptor apparatus. Receptor recruitment to inhibitory GABAergic and glycinergic synapses is controlled by the scaffold protein gephyrin and the adaptor protein collybistin. We derived new insights into the structure of collybistin and used these to design biochemical, cell biological, and genetic analyses of collybistin function. Our data define a collybistin-based protein interaction network that controls the gephyrin content of inhibitory postsynapses. Within this network, collybistin can adopt open/active and closed/inactive conformations to act as a switchable adaptor that links gephyrin to plasma membrane phosphoinositides. This function of collybistin is regulated by binding of the adhesion protein neuroligin-2, which stabilizes the open/active conformation of collybistin at the postsynaptic plasma membrane by competing with an intramolecular interaction in collybistin that favors the closed/inactive conformation. By linking trans-synaptic neuroligin-dependent adhesion and phosphoinositide signaling with gephyrin recruitment, the collybistin-based regulatory switch mechanism represents an integrating regulatory node in the formation and function of inhibitory postsynapses. PubMed: 25082542DOI: 10.15252/embj.201488143 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.5 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






