4YEB
Structural characterization of a synaptic adhesion complex
4YEB の概要
エントリーDOI | 10.2210/pdb4yeb/pdb |
関連するPDBエントリー | 4RMK 4RML |
分子名称 | Latrophilin-3, Fibronectin leucine rich transmembrane protein 3, CALCIUM ION, ... (4 entities in total) |
機能のキーワード | complex, latrophilin 3, flrt3, central nervous system, signaling protein |
由来する生物種 | Mus musculus (Mouse) 詳細 |
細胞内の位置 | Cell membrane; Multi-pass membrane protein: Q80TS3 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 78571.29 |
構造登録者 | Ranaivoson, F.M.,Liu, Q.,Martini, F.,Bergami, F.,von Daake, S.,Li, S.,Lee, D.,Demeler, B.,Hendrickson, W.A.,Comoletti, D. (登録日: 2015-02-23, 公開日: 2015-08-19, 最終更新日: 2024-10-16) |
主引用文献 | Ranaivoson, F.M.,Liu, Q.,Martini, F.,Bergami, F.,von Daake, S.,Li, S.,Lee, D.,Demeler, B.,Hendrickson, W.A.,Comoletti, D. Structural and Mechanistic Insights into the Latrophilin3-FLRT3 Complex that Mediates Glutamatergic Synapse Development. Structure, 23:1665-1677, 2015 Cited by PubMed Abstract: Latrophilins (LPHNs) are adhesion-like G-protein-coupled receptors implicated in attention-deficit/hyperactivity disorder. Recently, LPHN3 was found to regulate excitatory synapse number through trans interactions with fibronectin leucine-rich repeat transmembrane 3 (FLRT3). By isothermal titration calorimetry, we determined that only the olfactomedin (OLF) domain of LPHN3 is necessary for FLRT3 association. By multi-crystal native single-wavelength anomalous diffraction phasing, we determined the crystal structure of the OLF domain. This structure is a five-bladed β propeller with a Ca(2+) ion bound in the central pore, which is capped by a mobile loop that allows the ion to exchange with the solvent. The crystal structure of the OLF/FLRT3 complex shows that LPHN3-OLF in the closed state binds with high affinity to the concave face of FLRT3-LRR with a combination of hydrophobic and charged residues. Our study provides structural and functional insights into the molecular mechanism underlying the contribution of LPHN3/FLRT3 to the development of glutamatergic synapses. PubMed: 26235031DOI: 10.1016/j.str.2015.06.022 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.19 Å) |
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