1XOD

Crystal structure of X. tropicalis Spred1 EVH-1 domain

Summary for 1XOD

• Entry DOI: 10.2210/pdb1xod/pdb
• Descriptor: Spred1, GLYCEROL (3 entities in total)
• Functional Keywords: spred, sprouty, evh1, peptide-binding, signaling protein
• Biological source: Xenopus tropicalis (western clawed frog)
• Cellular location: Membrane; Peripheral membrane protein (By similarity): Q66JG9
• Total number of polymer chains: 2
• Total formula weight: 26033.17

Authors

Harmer, N.J.,Sivak, J.M.,Amaya, E.,Blundell, T.L. (deposition date: 2004-10-06, release date: 2005-01-25, Last modification date: 2023-08-23)

Primary citation

Harmer, N.J.,Sivak, J.M.,Amaya, E.,Blundell, T.L.
1.15A Crystal structure of the X. tropicalis Spred1 EVH1 domain suggests a fourth distinct peptide-binding mechanism within the EVH1 family
Febs Lett., 579:1161-1166, 2005

PubMed 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.

PubMed: 15710406
DOI: 10.1016/j.febslet.2004.11.114

Experimental method

X-RAY DIFFRACTION (1.15 Å)