1SHX

Ephrin A5 ligand structure

1SHX の概要

• エントリーDOI: 10.2210/pdb1shx/pdb
• 関連するPDBエントリー: 1shw
• 関連するBIRD辞書のPRD_ID: PRD_900017
• 分子名称: Ephrin-A5, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: ephrin signaling, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33692.66

構造登録者

Himanen, J.P.,Barton, W.A.,Nikolov, D.B.,Jeffrey, P.D. (登録日: 2004-02-26, 公開日: 2005-04-19, 最終更新日: 2024-11-20)

主引用文献

Day, B.,To, C.,Himanen, J.P.,Smith, F.M.,Nikolov, D.B.,Boyd, A.W.,Lackmann, M.
Three distinct molecular surfaces in ephrin-A5 are essential for a functional interaction with EphA3.
J.Biol.Chem., 280:26526-26532, 2005

PubMed Abstract: Eph receptor tyrosine kinases (Ephs) function as molecular relays that interact with cell surface-bound ephrin ligands to direct the position of migrating cells. Structural studies revealed that, through two distinct contact surfaces on opposite sites of each protein, Eph and ephrin binding domains assemble into symmetric, circular heterotetramers. However, Eph signal initiation requires the assembly of higher order oligomers, suggesting additional points of contact. By screening a random library of EphA3 binding-compromised ephrin-A5 mutants, we have now determined ephrin-A5 residues that are essential for the assembly of high affinity EphA3 signaling complexes. In addition to the two interfaces predicted from the crystal structure of the homologous EphB2.ephrin-B2 complex, we identified a cluster of 10 residues on the ephrin-A5 E alpha-helix, the E-F loop, the underlying H beta-strand, as well as the nearby B-C loop, which define a distinct third surface required for oligomerization and activation of EphA3 signaling. Together with a corresponding third surface region identified recently outside of the minimal ephrin binding domain of EphA3, our findings provide experimental evidence for the essential contribution of three distinct protein-interaction interfaces to assemble functional EphA3 signaling complexes.

PubMed: 15901737
DOI: 10.1074/jbc.M504972200

実験手法

X-RAY DIFFRACTION (2.1 Å)