Ephrin, ligand binding domain
IPR001090
Definition
The Eph LBD domain forms a compact globular structure which folds into a jellyroll β-sandwich composed of 11 antiparallel β-strands. It has two antiparallel β-sheets, with the usual left-handed twist, packed against each other to form a compact β-sandwich, and a short 3(10) helix [[cite:PMID:9853759], [cite:PMID:11780069], [cite:PMID:19525919]]. The Eph receptors, which bind a group of cell-membrane-anchored ligands known as ephrins, represent the largest subfamily of receptor tyrosine kinases (RTKs). These receptors and their ephrin ligands control a diverse array of cell-cell interactions in the nervous and vascular systems. Upon ephrin binding, the Eph kinase domain is activated, initiating "forward" signalling in the receptor-expressing cells. Simultaneously, signals are induced in the ligand-expressing cells, a phenomenon referred to as "reverse" signalling. The extracellular region of Eph receptors contains a conserved 180-amino-acid N-terminal ligand-binding domain (LBD), which is both necessary and sufficient for binding to ephrin ligands. An adjacent cysteine-rich region may be involved in the receptor-receptor oligomerisation often observed upon ligand binding, whereas the two fibronectin type III repeats have yet to be assigned a clear biological function. The cytoplasmic region contains a kinase domain, a sterile alpha motif (SAM) domain, and a PDZ-binding motif. The LBD is unique to this family of RTKs and shares no significant amino acid sequence homology with other known proteins [[cite:PMID:9853759], [cite:PMID:11780069], [cite:PMID:19525919]]. The Eph LBD forms a compact globular structure that folds into a jellyroll β-sandwich composed of 11 antiparallel β-strands. Two antiparallel β-sheets with the typical left-handed twist pack against each other to form a compact β-sandwich, along with a short helix [[cite:PMID:9853759], [cite:PMID:11780069], [cite:PMID:19525919]].
14 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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