Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-2322
FEBS Lett 2005 Feb 14;5795:1161-6. doi: 10.1016/j.febslet.2004.11.114.
Show Gene links Show Anatomy links

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 .


???displayArticle.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.

???displayArticle.pubmedLink??? 15710406
???displayArticle.link??? FEBS Lett


Species referenced: Xenopus tropicalis
Genes referenced: spred1