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Specificity and affinity motifs for Grb2 SH2-ligand interactions
journal contribution
posted on 2002-06-25, 00:00 authored by H Kessels, Alister WardAlister Ward, T SchumacherProtein–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.
History
Journal
Proceedings of the National Academy of SciencesVolume
99Issue
13Pagination
8524 - 8529Publisher
National Academy of SciencesLocation
Washington, D.C.Publisher DOI
ISSN
0027-8424eISSN
1091-6490Language
engNotes
Journal edited by Joseph Schlessinger, Yale University School of Medicine, New Haven, CTPublication classification
C1.1 Refereed article in a scholarly journalCopyright notice
2002, National Academy of SciencesUsage metrics
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