Interaction of the non-phosphorylated peptide G7-18NATE with Grb7-SH2 domain requires phosphate for enhanced affinity and specificity
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology; Monash University; VIC; 3800; Australia
2. Department of Surgery and Vermont Cancer Center; University of Vermont; Burlington; VT; USA
Publisher
Wiley
Subject
Molecular Biology,Structural Biology
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/jmr.2148/fullpdf
Reference48 articles.
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2. Uptake of a cell permeable G7-18NATE construct into cells and binding with the Grb7-SH2 domain;Ambaye;Biopolymers,2011b
3. Structural basis of binding by cyclic non-phosphorylated peptide antagonists of Grb7 implicated in breast cancer progression;Ambaye;J. Mol. Biol.,2011c
4. GRB-7 facilitates HER-2/Neu-mediated signal transduction and tumor formation;Bai;Carcinogenesis,2008
5. Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide;Bradshaw;Biochemistry,1998
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