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| [[Image:1iko.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1iko| PDB=1iko | SCENE= }} | | {{STRUCTURE_1iko| PDB=1iko | SCENE= }} |
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| '''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN'''
| | ===CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_11703926}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 11703926 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_11703926}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Glycosylation]] | | [[Category: Glycosylation]] |
| [[Category: Greek key]] | | [[Category: Greek key]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 20:06:24 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 13:24:13 2008'' |