1iko
From Proteopedia
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| - | [[Image:1iko.gif|left|200px]] | + | [[Image:1iko.gif|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN''' | + | {{Structure |
| + | |PDB= 1iko |SIZE=350|CAPTION= <scene name='initialview01'>1iko</scene>, resolution 1.92Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= ephrin-B2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 Mus musculus]) | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IKO is a [ | + | 1IKO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IKO OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11703926 11703926] |
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: greek key]] | [[Category: greek key]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:36 2008'' |
Revision as of 09:51, 20 March 2008
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| , resolution 1.92Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | ephrin-B2 (Mus musculus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN
Overview
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 Structure
1IKO is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:51:36 2008
