1iko
CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN
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OverviewOverview
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.
About this StructureAbout this Structure
1IKO is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
ReferenceReference
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
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