| Structural highlights
6p7s is a 4 chain structure with sequence from Cedpv and Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | , |
| Gene: | Efnb1, Epl2, Eplg2, Lerk2, Stra1 (LK3 transgenic mice) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[EFNB1_MOUSE] Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development (PubMed:7929389, PubMed:10704386). Binding to Eph receptors residing on adjacent cells leads to contact-dependent bidirectional signaling into neighboring cells (PubMed:7929389, PubMed:10704386). Shows high affinity for the receptor tyrosine kinase EPHB1/ELK (By similarity). Can also bind EPHB2 and EPHB3 (PubMed:7929389). Binds to, and induces the collapse of, commissural axons/growth cones in vitro (PubMed:10704386). May play a role in constraining the orientation of longitudinally projecting axons (PubMed:10704386).[UniProtKB:P98172][1] [2]
Publication Abstract from PubMed
Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only approximately 30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.
Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.,Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi:, 10.1073/pnas.1911773116. Epub 2019 Sep 23. PMID:31548390[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Imondi R, Wideman C, Kaprielian Z. Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons. Development. 2000 Apr;127(7):1397-410. PMID:10704386
- ↑ Shao H, Lou L, Pandey A, Pasquale EB, Dixit VM. cDNA cloning and characterization of a ligand for the Cek5 receptor protein-tyrosine kinase. J Biol Chem. 1994 Oct 28;269(43):26606-9. PMID:7929389
- ↑ Laing ED, Navaratnarajah CK, Cheliout Da Silva S, Petzing SR, Xu Y, Sterling SL, Marsh GA, Wang LF, Amaya M, Nikolov DB, Cattaneo R, Broder CC, Xu K. Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. Proc Natl Acad Sci U S A. 2019 Oct 8;116(41):20707-20715. doi:, 10.1073/pnas.1911773116. Epub 2019 Sep 23. PMID:31548390 doi:http://dx.doi.org/10.1073/pnas.1911773116
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