1iko: Difference between revisions
New page: left|200px<br /><applet load="1iko" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iko, resolution 1.92Å" /> '''CRYSTAL STRUCTURE OF... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1iko.gif|left|200px]]<br /><applet load="1iko" size=" | [[Image:1iko.gif|left|200px]]<br /><applet load="1iko" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1iko, resolution 1.92Å" /> | caption="1iko, resolution 1.92Å" /> | ||
'''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN'''<br /> | '''CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Eph receptor tyrosine kinases and their membrane-associated ligands, the | 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== | ==About this Structure== | ||
1IKO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http:// | 1IKO is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
| Line 14: | Line 14: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bard, J.]] | [[Category: Bard, J.]] | ||
[[Category: Bethoney, K | [[Category: Bethoney, K A.]] | ||
[[Category: Cutforth, T.]] | [[Category: Cutforth, T.]] | ||
[[Category: Gelinas, A | [[Category: Gelinas, A D.]] | ||
[[Category: Harrison, C | [[Category: Harrison, C J.]] | ||
[[Category: Toth, J.]] | [[Category: Toth, J.]] | ||
[[Category: glycosylation]] | [[Category: glycosylation]] | ||
[[Category: greek key]] | [[Category: greek key]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:12:51 2008'' | ||
Revision as of 14:12, 21 February 2008
|
CRYSTAL STRUCTURE OF THE MURINE EPHRIN-B2 ECTODOMAIN
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
Page seeded by OCA on Thu Feb 21 13:12:51 2008