Two-Dimensional Diversity: Screening Human cDNA Phage Display Libraries with a Random Diversity Probe for the Display Cloning of Phosphotyrosine Binding Domains
- 1 March 2004
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (12) , 3730-3731
- https://doi.org/10.1021/ja039006p
Abstract
A random phosphopeptide probe (bio-pYZZZ) has been used for the isolation and identification of multiple SH2 domains from human cDNA-displaying phage libraries. In addition, on-phage analysis and quantification of binding affinities for these phage-displayed proteins has shown them to be functional domains, retaining the same characteristics as in their native state.Keywords
This publication has 5 references indexed in Scilit:
- Phosphotyrosine-binding domains in signal transductionNature Reviews Molecular Cell Biology, 2002
- Identification of natural ligands for SH2 domains from a phage display cDNA libraryJournal of Molecular Biology, 2000
- Mapping signal transduction pathways by phage displayNature Biotechnology, 1999
- Signaling Through Scaffold, Anchoring, and Adaptor ProteinsScience, 1997
- Binding of a high affinity phosphotyrosyl peptide to the Src SH2 domain: Crystal structures of the complexed and peptide-free formsCell, 1993