Ephrin receptor
| Eph receptor ligand binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
Structure of the kinase domain of human eph type-A receptor 5 (EphA5) | |||||||||
| Identifiers | |||||||||
| Symbol | Ephrin_lbd | ||||||||
| Pfam | PF01404 | ||||||||
| InterPro | IPR016257 | ||||||||
| SCOP2 | 1nuk / SCOPe / SUPFAM | ||||||||
| CDD | cd10319 | ||||||||
| Membranome | 1202 | ||||||||
| |||||||||
Eph receptors (Ephs, after erythropoietin-producing human hepatocellular receptors) are a group of receptors that are activated in response to binding with Eph receptor-interacting proteins (Ephrins). Ephs form the largest known subfamily of receptor tyrosine kinases (RTKs). Both Eph receptors and their corresponding ephrin ligands are membrane-bound proteins that require direct cell-cell interactions for Eph receptor activation. Eph/ephrin signaling has been implicated in the regulation of a host of processes critical to embryonic development including axon guidance, formation of tissue boundaries, cell migration, and segmentation. Additionally, Eph/ephrin signaling has been identified to play a critical role in the maintenance of several processes during adulthood including long-term potentiation, angiogenesis, and stem cell differentiation and cancer.