v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| 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 tothe membrane via a GPI linkage, while type-B ephrins are type-I membrane proteins.The globular ephrin receptor-binding domain (ephrin RBD) is a beta barrel composed of eight strands arranged in two sheets around a hydrophobic core. Interspersed between beta strands are two alpha helices andone 3(10) helix. The sheets are composed of mixed parallel and antiparallel beta strands arranged in a Greek key topology. Like other cell-surfaceproteins, ephrins contain disulfide bonds to enhance stability. Two buried disulfide bonds are present: one pair holds together beta strands C and F, andthe other pair anchors two small helices, E and I, at the top of the barrel [, ]. |
| Short Name | Ephrin_RBD |