Crystal Structure of an Ephrin Ectodomain
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. Multi...
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| Veröffentlicht in: | Developmental cell 2001-07, Vol.1 (1), p.83-92 |
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| container_title | Developmental cell |
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| creator | Toth, Joseph Cutforth, Tyler Gelinas, Amy D. Bethoney, Kelley A. Bard, Joel Harrison, Celia J. |
| description | 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 β 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. |
| doi_str_mv | 10.1016/S1534-5807(01)00002-8 |
| format | Article |
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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 β 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. 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| source | MEDLINE; Cell Press Free Archives; Access via ScienceDirect (Elsevier); EZB-FREE-00999 freely available EZB journals |
| subjects | Amino Acid Sequence Animals Binding Sites - genetics Crystallography Ephrin-B2 Ligands Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Mice Molecular Sequence Data Mutation, Missense Plant Proteins - chemistry Protein Structure, Quaternary Protein Structure, Tertiary |
| title | Crystal Structure of an Ephrin Ectodomain |
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