PROSITE documentation PDOC01003Ephrin receptor-binding (ephrin RBD) domain signature and profile
Ephrins are a family of proteins [1] that are ligands of class V (EPH-related) receptor protein-tyrosine kinases (see <PDOC00629>). 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 specialized epithelia [2].
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 β barrel composed of eight strands arranged in two sheets around a hydrophobic core (see <PDB:1IKO>). Interspersed between β strands are two α helices and one 3(10) helix. The sheets are composed of mixed parallel and antiparallel β 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 β strands C and F, and the other pair anchors two small helices, E and I, at the top of the barrel [2,3].
We developed both a pattern and a profile for the ephrin RBD domain. The profile covers the entire ephrin RBD domain.
Last update:October 2011 / Text revised; profile added.
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PROSITE methods (with tools and information) covered by this documentation:
| 1 | Authors | Kozlosky C.J. Maraskovsky E. McGrew J.T. Vandenbos T. Teepe M. Lyman S.D. Srinivasan S. Fletcher F.A. Gayle R.B. III Cerretti D.P. Beckmann M.P. |
| Title | Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins. | |
| Source | Oncogene 10:299-306(1995). | |
| PubMed ID | 7838529 |
| 2 | Authors | Himanen J.-P. Rajashankar K.R. Lackmann M. Cowan C.A. Henkemeyer M. Nikolov D.B. |
| Title | Crystal structure of an Eph receptor-ephrin complex. | |
| Source | Nature 414:933-938(2001). | |
| PubMed ID | 11780069 | |
| DOI | 10.1038/414933a |
| 3 | Authors | Toth J. Cutforth T. Gelinas A.D. Bethoney K.A. Bard J. Harrison C.J. |
| Title | Crystal structure of an ephrin ectodomain. | |
| Source | Dev. Cell 1:83-92(2001). | |
| PubMed ID | 11703926 |
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