Ephrin receptor-binding domain (IPR001799)

Short name: Ephrin_RBD

Overlapping homologous superfamilies

Domain relationships


Ephrins are a family of proteins [PMID: 7838529] 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 [PMID: 11780069].

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 beta barrel composed of eight strands arranged in two sheets around a hydrophobic core. Interspersed between beta strands are two alpha helices and one 3(10) helix. The sheets are composed of mixed parallel and antiparallel beta 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 beta strands C and F, and the other pair anchors two small helices, E and I, at the top of the barrel [PMID: 11780069, PMID: 11703926].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

No terms assigned in this category.

Cellular Component

GO:0016020 membrane

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles