Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10873666 | FEBS Letters | 2005 | 6 Pages |
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 1.15Â Ã
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 β-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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Authors
Nicholas J. Harmer, Jeremy M. Sivak, Enrique Amaya, Tom L. Blundell,