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

Summary: 1.15 A Crystal structure of the X. tropicalis Spred1 EVH1 domain
suggests a fourth distinct peptide-binding mechanism
within the EVH1 familyq
Nicholas J. Harmera,*, Jeremy M. Sivakb
, Enrique Amayab
, Tom L. Blundella
a
Department of Biochemistry, 80 Tennis Court Road, Cambridge, CB2 1GA, UK
b
Wellcome Trust/Cancer Research UK Gurdon Institute, Tennis Court Road, Cambridge, CB2 1QR, UK
Received 6 October 2004; revised 19 November 2004; accepted 22 November 2004
Available online 19 January 2005
Edited by Hans Eklund
Abstract The recently described Spred protein family has been
implicated in the modulation of receptor tyrosine kinase signal-
ling. We report the crystal structure of the Enabled/vasodila-
tor-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 pleck-
strin-homology fold, with a similar secondary structure to

  

Source: Amaya, Enrique - Healing Foundation Centre & Developmental Biology, Faculty of Life Sciences, University of Manchester

 

Collections: Biology and Medicine