Ligand ephrin

Gerety, S. S. et al. (1999). Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. Mol. Cell 4, 403-414. 

Fasanaro P, D Alessandra Y, Di Stefano V, Melchionna R, Romani S, Pompilio G, Capogrossi MC, Martelli F (2008) MicroRNA-210 modulates endothelial cell response to hypoxia and inhibits the receptor tyrosine kinase ligand ephrin-A3. J Biol Chem 283(23) 15878-15883... 

Ephrins are a group of membranous ligands, which function through a family of receptor tyrosine kinases (Ephs). Ephrin/Eph-mediated signaling processes are involved in morphogenetic processes taking place e.g. during the development of the nervous system or the vasculature. 

Myshkin, E. and Wang, B. Chemometrical classification of ephrin ligands and eph kinases using GRID/CPCAapproach./. Chem. Inf. Comput. Sci. 2003, 43, 1004-1010. 

Fig. 2. Structures of the extracellular domains of Ephs and ephrins. The molecular surfaces (semi-transparent) are also indicated. (A) Structure of the ligand-binding domain of EphB2. The N- and C-termini of the molecule are labeled, as are the class-specificity loop (H-I) and the ligand-binding loops that are largely disordered in the absence of bound ephrin. (B) Structure of the extracellular receptor-binding domain of ephrin-B2. Indicated is the location of the receptor-binding G-H loop. (C) Structure of the EphB2/ephrin-B2 tetramer. Eph receptors are blue and ephrins are green. The high-affinity dimerization interfaces are indicated by arrows. (See Color Insert.)...

Fig. 4. Structures of the Eph/ephrin intra- and inter-subclass heterodimers. (A) Structure of the EphB2 (right)/ephrin-B2 (left) high-affinity heterodimer. The N- and C-termini of the molecules are indicated. (B) Structure of the complex between EphB2 and ephrin-A5 in the same orientation as in (A). The arrows indicate the changes in the relative ligand and receptor positions between the intra- and inter-subclass complexes.

Dodelet, V. C., and Pasquale, E. B. (2000). Eph receptors and ephrin ligands Embryo-genesis to tumorigenesis. Oncogene 19, 5614—5619. 

Song, J. et al. (2002). Solution structure and backbone dynamics of the functional cytoplasmic subdomain of human ephrin b2, a cell-surface ligand with bi-directional signaling properties. Biochemistry 41, 10942-10949. 

Torres, R. et al. (1998). PDZ proteins bind, cluster, and synaptically colocalize with Eph receptors and their ephrin ligands. Neuron 21, 1453-1463. 

Eph receptor tyrosine kinases play a crucial role in intercellular processes such as angiogenesis, neurogenesis, and carcinogenesis. Based on their affinity for ephrin ligands, the Eph kinases are divided into two subfamilies, EphA and EphB, which bind to ephrinA and ephrinB, respectively [60]. 

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