Specificity and affinity motifs for Grb2 SH2-ligand interactions

Kessels, Helmut W. H. G., Ward, Alister and Schumacher, Ton N. M. 2002, Specificity and affinity motifs for Grb2 SH2-ligand interactions, Proceedings of the National Academy of Sciences, vol. 99, no. 13, pp. 8524-8529.

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Title Specificity and affinity motifs for Grb2 SH2-ligand interactions
Author(s) Kessels, Helmut W. H. G.
Ward, Alister
Schumacher, Ton N. M.
Journal name Proceedings of the National Academy of Sciences
Volume number 99
Issue number 13
Start page 8524
End page 8529
Publisher National Academy of Sciences
Place of publication Washington, D.C.
Publication date 2002-06-25
ISSN 0027-8424
1091-6490
Summary Protein–protein interactions are often mediated by the recognition of short continuous amino acid stretches on target proteins by specific binding domains. Affinity-based selection strategies have successfully been used to define recognition motifs for a large series of such protein domains. However, in many biological systems specificity of interaction may be of equal or greater importance than affinity. To address this issue we have developed a peptide library screening technology that can be used to directly define ligands for protein domains based on both affinity and specificity of interaction. We demonstrate the value of this approach by the selection of peptide ligands that are either highly specific for the Grb2 Src homology 2 (SH2) domain or that are cross-reactive between a group of related SH2 domains. Examination of previously identified physiological ligands for the Grb2 SH2 domain suggests that for these ligands regulation of the specificity of interaction may be an important factor for in vivo ligand selection.
Notes Journal edited by Joseph Schlessinger, Yale University School of Medicine, New Haven, CT
Language eng
Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2002, National Academy of Sciences
Persistent URL http://hdl.handle.net/10536/DRO/DU:30006558

Document type: Journal Article
Collection: School of Biological and Chemical Sciences
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