1.15Å Crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family

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

FEBS Letters 579:1161-1166 (2005) (Full Article, 484Kb).

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 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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