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PROSITE documentation PDOC01003 [for PROSITE entry PS01299]

Ephrin 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.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

EPHRIN_RBD_1, PS01299; Ephrin receptor-binding (ephrin RBD) domain signature  (PATTERN)

EPHRIN_RBD_2, PS51551; Ephrin receptor-binding (ephrin RBD) domain profile  (MATRIX)


1AuthorsKozlosky 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.
TitleLigands for the receptor tyrosine kinases hek and elk: isolation of cDNAs encoding a family of proteins.
SourceOncogene 10:299-306(1995).
PubMed ID7838529

2AuthorsHimanen J.-P. Rajashankar K.R. Lackmann M. Cowan C.A. Henkemeyer M. Nikolov D.B.
TitleCrystal structure of an Eph receptor-ephrin complex.
SourceNature 414:933-938(2001).
PubMed ID11780069

3AuthorsToth J. Cutforth T. Gelinas A.D. Bethoney K.A. Bard J. Harrison C.J.
TitleCrystal structure of an ephrin ectodomain.
SourceDev. Cell 1:83-92(2001).
PubMed ID11703926

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