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1xod

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(New page: 200px<br /><applet load="1xod" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xod, resolution 1.15&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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.]]
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[[Category: Blundell, T.L.]]
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[[Category: Blundell, T L.]]
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[[Category: Harmer, N.J.]]
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[[Category: Harmer, N J.]]
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[[Category: Sivak, J.M.]]
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[[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://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:14:10 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:56:56 2008''

Revision as of 13:56, 21 February 2008

Image:1xod.gif

1xod, resolution 1.15Å

Drag the structure with the mouse to rotate

Crystal structure of X. tropicalis Spred1 EVH-1 domain

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.

About this Structure

1XOD is a Single protein structure of sequence from Xenopus tropicalis with as ligand. Full crystallographic information is available from OCA.

Reference

1.15 A crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family., Harmer NJ, Sivak JM, Amaya E, Blundell TL, FEBS Lett. 2005 Feb 14;579(5):1161-6. PMID:15710406

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