Ephrin-A5

Ephrin-A5 is a glycosylphosphatidylinositol ("GPI")-anchored cell surface ligand that binds Eph receptor tyrosine kinases, notably EphA4, EphA3, and EPHB2, triggering signal transduction pathways that influence cell attachment, morphology, migration, and pathfinding, with major roles in the nervous and vascular systems[1][2][3][5][6]. The structure of ephrin-A5 is characterized by a Greek key β-barrel fold stabilized by disulfide bonds, and its interaction with Eph receptors involves high-affinity binding mediated by the exposed G–H loop, which undergoes a conformational change upon receptor engagement[1][3][7]. Ephrin-A5 signaling regulates cell adhesion and morphology by activating integrins and downstream kinases like Src and ERK, and is considered a candidate target for cancer therapeutics and neurodevelopmental research[1][5][7].

Other names

EFNA5Ephrin-A5 ligand

Drugs may act as antagonists or inhibitors, targeting the G–H loop or blocking high-affinity Eph/ephrin interaction