1iko

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CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN

Structural highlights

1iko is a 1 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.92Å
Ligands:MAN, NAG
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EFNB2_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. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. Binds to receptor tyrosine kinase including EPHA4, EPHA3 and EPHB4. Together with EPHB4 plays a central role in heart morphogenesis and angiogenesis through regulation of cell adhesion and cell migration. EPHB4-mediated forward signaling controls cellular repulsion and segregation from EFNB2-expressing cells. May play a role in constraining the orientation of longitudinally projecting axons.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Eph receptor tyrosine kinases and their membrane-associated ligands, the ephrins, are essential regulators of axon guidance, cell migration, segmentation, and angiogenesis. There are two classes of vertebrate ephrin ligands which have distinct binding specificities for their cognate receptors. Multimerization of the ligands is required for receptor activation, and ephrin ligands themselves signal intracellularly upon binding Eph receptors. We have determined the structure of the extracellular domain of mouse ephrin-B2. The ephrin ectodomain is an eight-stranded beta barrel with topological similarity to plant nodulins and phytocyanins. Based on the structure, we have identified potential surface determinants of Eph/ephrin binding specificity and a ligand dimerization region. The high sequence similarity among ephrin ectodomains indicates that all ephrins may be modeled upon the ephrin-B2 structure presented here.

Crystal structure of an ephrin ectodomain.,Toth J, Cutforth T, Gelinas AD, Bethoney KA, Bard J, Harrison CJ Dev Cell. 2001 Jul;1(1):83-92. PMID:11703926[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
25 reviews cite this structure
Mechanisms and functions of Eph and ephrin signalling.
Kullander et al. (2002)
24 more
38 other articles
No citations found

See Also

References

  1. ↑ Toth J, Cutforth T, Gelinas AD, Bethoney KA, Bard J, Harrison CJ. Crystal structure of an ephrin ectodomain. Dev Cell. 2001 Jul;1(1):83-92. PMID:11703926

Contents


PDB ID 1iko

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OCA

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