Domain

Ephrin receptor ligand binding domain (IPR001090)

Short name: Ephrin_rcpt_lig-bd_dom

Domain relationships

Description

The Eph receptors, which bind a group of cell-membrane-anchored ligands known as ephrins, represent the largest subfamily of receptor tyrosine kinases (RTKs). The Eph receptors and their ephrin ligands control a diverse array of cell-cell interactions in the nervous and vascular systems. On ephrin binding, the Eph kinase domain is activated, initiating 'forward' signaling in the receptor-expressing cells. Simultaneously, signals are also induced in the ligand-expressing cells a phenomenon referred to as 'reverse' signalling. The extracellular Eph receptor region contains a conserved 180- amino-acid N-terminal ligand-binding domain (LBD) which is both necessary and sufficient for bindings of the receptors to their ephrin ligands. An adjacent cysteine-rich region might be involved in receptor-receptor oligomerization often observed on ligand binding, whereas the next two fibronectin type III repeats have yet to be assigned a clear biological function. The cytoplasmic Eph receptor region contains a kinase domain, a sterile alpha motif (SAM) domain, and a PDZ-binding motif. The ligand-binding domain (LBD) of Eph receptors is unique to this family of RTKs ans shares no significant amino-acid-sequence homology with other known proteins [PMID: 9853759, PMID: 11780069, PMID: 19525919].

The Eph LBD domain forms a compact globular structure which folds into a jellyroll beta-sandwich composed of 11 antiparallel beta-strands. It has two antiparallel beta-sheets, with the usual left-handed twist, packed against each other to form a compact beta-sandwich, and a short 3(10) helix [PMID: 9853759, PMID: 11780069, PMID: 19525919].

GO terms

Biological Process

GO:0048013 ephrin receptor signaling pathway

Molecular Function

No terms assigned in this category.

Cellular Component

No terms assigned in this category.

Contributing signatures

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