2WO1

Crystal Structure of the EphA4 Ligand Binding Domain

2WO1 の概要

• エントリーDOI: 10.2210/pdb2wo1/pdb
• 関連するPDBエントリー: 2WO2 2WO3
• 分子名称: EPHRIN TYPE-A RECEPTOR, N-PROPANOL (3 entities in total)
• 機能のキーワード: glycoprotein, axon guidance, vascular development, cell surface receptor, transferase, cell signaling
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Cell membrane ; Single-pass type I membrane protein : P54764
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43234.86

構造登録者

Bowden, T.A.,Aricescu, A.R.,Nettleship, J.E.,Siebold, C.,Rahman-Huq, N.,Owens, R.J.,Stuart, D.I.,Jones, E.Y. (登録日: 2009-07-21, 公開日: 2009-10-27, 最終更新日: 2024-10-09)

主引用文献

Bowden, T.A.,Aricescu, A.R.,Nettleship, J.E.,Siebold, C.,Rahman-Huq, N.,Owens, R.J.,Stuart, D.I.,Jones, E.Y.
Structural Plasticity of Eph-Receptor A4 Facilitates Cross-Class Ephrin Signalling
Structure, 17:1386-, 2009

PubMed Abstract: The EphA4 tyrosine kinase cell surface receptor regulates an array of physiological processes and is the only currently known class A Eph receptor that binds both A and B class ephrins with high affinity. We have solved the crystal structure of the EphA4 ligand binding domain alone and in complex with (1) ephrinB2 and (2) ephrinA2. This set of structures shows that EphA4 has significant conformational plasticity in its ligand binding face. In vitro binding data demonstrate that it has a higher affinity for class A than class B ligands. Structural analyses, drawing on previously reported Eph receptor structures, show that EphA4 in isolation and in complex with ephrinA2 resembles other class A Eph receptors but on binding ephrinB2 assumes structural hallmarks of the class B Eph receptors. This interactive plasticity reveals EphA4 as a structural chameleon, able to adopt both A and B class Eph receptor conformations, and thus provides a molecular basis for EphA-type cross-class reactivity.

PubMed: 19836338
DOI: 10.1016/J.STR.2009.07.018

実験手法

X-RAY DIFFRACTION (1.85 Å)