| Description | Ephrins are a family of proteins [ ] that are ligands of class V (EPH-related) receptor protein-tyrosine kinases. Initially identified as regulators of axon pathfinding and neuronal cell migration, the Eph receptors and their ephrin ligands are now known to have roles in many other cell-cell interactions, including those of vascular endothelial cells and specialised epithelia [].Ephrins are membrane-attached proteins of 205 to 340 residues. Attachment appears to be crucial for their normal function. Type-A ephrins are linked to the membrane via a GPI linkage, while type-B ephrins are type-I membrane proteins.The globular ephrin receptor-binding domain (ephrin RBD) is a β barrel composed of eight strands arranged in two sheets around a hydrophobic core. Interspersed between β strands are two α helices and one 3(10) helix. The sheets are composed of mixed parallel and antiparallel β strands arranged in a Greek key topology. Like other cell-surface proteins, ephrins contain disulfide bonds to enhance stability. Two buried disulfide bonds are present: one pair holds together β strands C and F, and the other pair anchors two small helices, E and I, at the top of the barrel [ , ]. | Name | Ephrin receptor-binding domain |
| Short Name | Ephrin_RBD | Type | Domain |
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