2GY5

Tie2 Ligand-Binding Domain Crystal Structure

2GY5 の概要

• エントリーDOI: 10.2210/pdb2gy5/pdb
• 関連するPDBエントリー: 2gy7
• 分子名称: Angiopoietin-1 receptor, 2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-alpha-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: ligand-binding domain, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: Q02763
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48676.44

構造登録者

Barton, W.A.,Nikolov, D.B. (登録日: 2006-05-09, 公開日: 2006-06-06, 最終更新日: 2024-10-30)

主引用文献

Barton, W.A.,Tzvetkova-Robev, D.,Miranda, E.P.,Kolev, M.V.,Rajashankar, K.R.,Himanen, J.P.,Nikolov, D.B.
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
Nat.Struct.Mol.Biol., 13:524-532, 2006

PubMed Abstract: The Tie receptor tyrosine kinases and their angiopoietin (Ang) ligands play central roles in developmental and tumor-induced angiogenesis. Here we present the crystal structures of the Tie2 ligand-binding region alone and in complex with Ang2. In contrast to prediction, Tie2 contains not two but three immunoglobulin (Ig) domains, which fold together with the three epidermal growth factor domains into a compact, arrowhead-shaped structure. Ang2 binds at the tip of the arrowhead utilizing a lock-and-key mode of ligand recognition-unique for a receptor kinase-where two complementary surfaces interact with each other with no domain rearrangements and little conformational change in either molecule. Ang2-Tie2 recognition is similar to antibody-protein antigen recognition, including the location of the ligand-binding site within the Ig fold. Analysis of the structures and structure-based mutagenesis provide insight into the mechanism of receptor activation and support the hypothesis that all angiopoietins interact with Tie2 in a structurally similar manner.

PubMed: 16732286
DOI: 10.1038/nsmb1101

実験手法

X-RAY DIFFRACTION (2.9 Å)