Ephrin type-B receptor 2 is a protein that in humans is encoded by the EPHB2 gene.[1]
Ephrin receptors and their ligands, the ephrins, mediate numerous developmental processes, particularly in the nervous system. Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. The Eph family of receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. Ephrin receptors make up the largest subgroup of the receptor tyrosine kinase (RTK) family. The protein encoded by this gene is a receptor for ephrin-B family members.[2]
Interactions
EPH receptor B2 has been shown to interact with Src,[3][4] RAS p21 protein activator 1[5][4] and the Abl gene.[6]
References
- ^ Chan J, Watt VM (Aug 1991). "eek and erk, new members of the eph subclass of receptor protein-tyrosine kinases". Oncogene 6 (6): 1057–61. PMID 1648701.
- ^ "Entrez Gene: EPHB2 EPH receptor B2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2048.
- ^ Zisch, A H; Kalo M S, Chong L D, Pasquale E B (May. 1998). "Complex formation between EphB2 and Src requires phosphorylation of tyrosine 611 in the EphB2 juxtamembrane region". Oncogene (ENGLAND) 16 (20): 2657–70. doi:10.1038/sj.onc.1201823. ISSN 0950-9232. PMID 9632142.
- ^ a b Zisch, A H; Pazzagli C, Freeman A L, Schneller M, Hadman M, Smith J W, Ruoslahti E, Pasquale E B (Jan. 2000). "Replacing two conserved tyrosines of the EphB2 receptor with glutamic acid prevents binding of SH2 domains without abrogating kinase activity and biological responses". Oncogene (ENGLAND) 19 (2): 177–87. doi:10.1038/sj.onc.1203304. ISSN 0950-9232. PMID 10644995.
- ^ Holland, S J; Gale N W, Gish G D, Roth R A, Songyang Z, Cantley L C, Henkemeyer M, Yancopoulos G D, Pawson T (Jul. 1997). "Juxtamembrane tyrosine residues couple the Eph family receptor EphB2/Nuk to specific SH2 domain proteins in neuronal cells". EMBO J. (ENGLAND) 16 (13): 3877–88. doi:10.1093/emboj/16.13.3877. ISSN 0261-4189. PMID 9233798.
- ^ Yu, H H; Zisch A H, Dodelet V C, Pasquale E B (Jul. 2001). "Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor". Oncogene (England) 20 (30): 3995–4006. doi:10.1038/sj.onc.1204524. ISSN 0950-9232. PMID 11494128.
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1b4f: OLIGOMERIC STRUCTURE OF THE HUMAN EPHB2 RECEPTOR SAM DOMAIN
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1f0m: MONOMERIC STRUCTURE OF THE HUMAN EPHB2 SAM (STERILE ALPHA MOTIF) DOMAIN
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1jpa: Crystal Structure of unphosphorylated EphB2 receptor tyrosine kinase and juxtamembrane region
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1kgy: Crystal Structure of the EphB2-ephrinB2 complex
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1nuk: CRYSTAL STRUCTURE OF THE LIGAND-BINDING DOMAIN OF THE EPHB2 RECEPTOR TYROSINE KINASE
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1sgg: THE SOLUTION STRUCTURE OF SAM DOMAIN FROM THE RECEPTOR TYROSINE KINASE EPHB2, NMR, 10 STRUCTURES
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1shw: EphB2 / EphrinA5 Complex Structure
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2hen: Crystal Structure of the EphB2 Receptor Kinase domain in complex with ADP
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