1iko: Difference between revisions

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[[Image:1iko.gif|left|200px]]
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{{STRUCTURE_1iko|  PDB=1iko  |  SCENE=  }}  
{{STRUCTURE_1iko|  PDB=1iko  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN'''
===CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN===




==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.
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==About this Structure==
==About this Structure==
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[[Category: Glycosylation]]
[[Category: Glycosylation]]
[[Category: Greek key]]
[[Category: Greek key]]
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Revision as of 13:24, 1 July 2008

File:1iko.png

Template:STRUCTURE 1iko

CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAINCRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN

Template:ABSTRACT PUBMED 11703926

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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