4RMK

Crystal structure of the Olfactomedin domain of latrophilin 3 in P65 crystal form

4RMK の概要

• エントリーDOI: 10.2210/pdb4rmk/pdb
• 関連するPDBエントリー: 4RML
• 分子名称: Latrophilin-3, CALCIUM ION (3 entities in total)
• 機能のキーワード: five-bladed beta-propeller, trans-synaptic adhesion gpcr, flrt3, central nervous system, signaling protein
• 由来する生物種: Mus musculus (mouse)
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : Q80TS3
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36672.65

構造登録者

Ranaivoson, F.M.,Liu, Q.,Martini, F.,Bergami, F.,Von daake, S.,Li, S.,Demeler, B.,Hendrickson, W.A.,Comoletti, D. (登録日: 2014-10-21, 公開日: 2015-08-19, 最終更新日: 2024-11-06)

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

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: 26235031
DOI: 10.1016/j.str.2015.06.022

実験手法

X-RAY DIFFRACTION (1.606 Å)