1.15 Å Crystal structure of theX. tropicalisSpred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family
- 19 January 2005
- journal article
- Published by Wiley in FEBS Letters
- Vol. 579 (5) , 1161-1166
- https://doi.org/10.1016/j.febslet.2004.11.114
Abstract
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.Keywords
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