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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 1.15Å" /> '''Crystal structure of...)
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Revision as of 04:06, 21 November 2007
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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 GOL 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
Page seeded by OCA on Wed Nov 21 06:14:10 2007
Categories: Single protein | Xenopus tropicalis | Amaya, E. | Blundell, T.L. | Harmer, N.J. | Sivak, J.M. | GOL | Evh1 | Peptide-binding | Spred | Sprouty
