1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR001426 | Conserved_site | Tyrosine-protein kinase, receptor class V, conserved site |
| Type: | Domain | Name: | Ephrin receptor ligand binding domain |
| 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 alsoinduced 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 adjacentcysteine-rich region might be involved in receptor-receptor oligomerization often observed on ligand binding, whereas the next two fibronectin type IIIrepeats 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 tothis family of RTKs ans shares no significant amino-acid-sequence homology with other known proteins [, , ].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-handedtwist, packed against each other to form a compact beta-sandwich, and a short 3(10) helix [, , ]. | Short Name: | Ephrin_rcpt_lig-bd_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR001426 | Conserved_site | Tyrosine-protein kinase, receptor class V, conserved site |
