1.15Å Crystal structure of the X. tropicalis Spred1 Enabled/Vasodilator-stimulated phosphoprotein homology-1 domain

Harmer, N.J. Sivak, J. Amaya, E. and Blundell, T.L.

FEBS Letters 579:1161-1166 (2005)

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 1.15Å 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.

© 2005 Federation of European Biochemical Societies

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