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'''Crystal structure of X. tropicalis Spred1 EVH-1 domain''' | '''Crystal structure of X. tropicalis Spred1 EVH-1 domain''' | ||
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[[Category: Harmer, N J.]] | [[Category: Harmer, N J.]] | ||
[[Category: Sivak, J M.]] | [[Category: Sivak, J M.]] | ||
[[Category: | [[Category: Evh1]] | ||
[[Category: | [[Category: Peptide-binding]] | ||
[[Category: | [[Category: Spred]] | ||
[[Category: | [[Category: Sprouty]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:17:38 2008'' | |||
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Revision as of 12:17, 3 May 2008
Crystal structure of X. tropicalis Spred1 EVH-1 domain
Overview
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.
About this Structure
1XOD is a Single protein structure of sequence from Xenopus tropicalis. Full crystallographic information is available from OCA.
Reference
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, FEBS Lett. 2005 Feb 14;579(5):1161-6. PMID:15710406 Page seeded by OCA on Sat May 3 15:17:38 2008
