1xod: Difference between revisions

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New page: left|200px<br /><applet load="1xod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xod, resolution 1.15Å" /> '''Crystal structure of...
 
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[[Image:1xod.gif|left|200px]]<br /><applet load="1xod" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1xod.gif|left|200px]]<br /><applet load="1xod" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1xod, resolution 1.15&Aring;" />
caption="1xod, resolution 1.15&Aring;" />
'''Crystal structure of X. tropicalis Spred1 EVH-1 domain'''<br />
'''Crystal structure of X. tropicalis Spred1 EVH-1 domain'''<br />


==Overview==
==Overview==
The recently described Spred protein family has been implicated in the, modulation of receptor tyrosine kinase signalling. We report the crystal, structure of the Enabled/vasodilator-stimulated phosphoprotein homology-1, (EVH1) domain from Xenopus tropicalis Spred1, solved to 1.15 A resolution., This structure confirms that the Spred EVH1 adopts the pleckstrin-homology, fold, with a similar secondary structure to Enabled. A translation of one, of the peptide-binding groove beta-strands narrows this groove, whilst one, end of the groove shows structural flexibility. We propose that Spred1, will bind peptides that are less proline-rich than other EVH1 domains, with conformational changes indicating an induced fit.
The recently described Spred protein family has been implicated in the modulation of receptor tyrosine kinase signalling. We report the crystal structure of the Enabled/vasodilator-stimulated phosphoprotein homology-1 (EVH1) domain from Xenopus tropicalis Spred1, solved to 1.15 A resolution. This structure confirms that the Spred EVH1 adopts the pleckstrin-homology fold, with a similar secondary structure to Enabled. A translation of one of the peptide-binding groove beta-strands narrows this groove, whilst one end of the groove shows structural flexibility. We propose that Spred1 will bind peptides that are less proline-rich than other EVH1 domains, with conformational changes indicating an induced fit.


==About this Structure==
==About this Structure==
1XOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis] with GOL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XOD OCA].  
1XOD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_tropicalis Xenopus tropicalis] with <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XOD OCA].  


==Reference==
==Reference==
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[[Category: Xenopus tropicalis]]
[[Category: Xenopus tropicalis]]
[[Category: Amaya, E.]]
[[Category: Amaya, E.]]
[[Category: Blundell, T.L.]]
[[Category: Blundell, T L.]]
[[Category: Harmer, N.J.]]
[[Category: Harmer, N J.]]
[[Category: Sivak, J.M.]]
[[Category: Sivak, J M.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: evh1]]
[[Category: evh1]]
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[[Category: sprouty]]
[[Category: sprouty]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:56 2008''