1NU2

Crystal structure of the murine Disabled-1 (Dab1) PTB domain-ApoER2 peptide-PI-4,5P2 ternary complex

1NU2 の概要

• エントリーDOI: 10.2210/pdb1nu2/pdb
• 関連するPDBエントリー: 1NTV
• 分子名称: Disabled homolog 1, peptide derived from murine Apolipoprotein E Receptor-2, D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: beta-sandwich, signaling protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 18760.24

構造登録者

Stolt, P.C.,Jeon, H.,Song, H.K.,Herz, J.,Eck, M.J.,Blacklow, S.C. (登録日: 2003-01-30, 公開日: 2003-04-15, 最終更新日: 2024-03-13)

主引用文献

Stolt, P.C.,Jeon, H.,Song, H.K.,Herz, J.,Eck, M.J.,Blacklow, S.C.
Origins of Peptide Selectivity and Phosphoinositide Binding Revealed by Structures of Disabled-1 PTB Domain Complexes
Structure, 11:569-579, 2003

PubMed Abstract: Formation of the mammalian six-layered neocortex depends on a signaling pathway that involves Reelin, the very low-density lipoprotein receptor, the apolipoprotein E receptor-2 (ApoER2), and the adaptor protein Disabled-1 (Dab1). The 1.5 A crystal structure of a complex between the Dab1 phosphotyrosine binding (PTB) domain and a 14-residue peptide from the ApoER2 tail explains the unusual preference of Dab1 for unphosphorylated tyrosine within the NPxY motif of the peptide. Crystals of the complex soaked with the phosphoinositide PI-4,5P(2) (PI) show that PI binds to conserved basic residues on the PTB domain opposite the peptide binding groove. This finding explains how the Dab1 PTB domain can simultaneously bind PI and the ApoER2 tail. Recruitment of the Dab1 PTB domain to PI-rich regions of the plasma membrane may facilitate association with the Reelin receptor cytoplasmic tails to transduce a critical positional cue to migrating neurons.

PubMed: 12737822
DOI: 10.1016/S0969-2126(03)00068-6

実験手法

X-RAY DIFFRACTION (1.9 Å)