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Related Concept Videos

Conservation of Protein Domains Over Different Proteins02:26

Conservation of Protein Domains Over Different Proteins

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Related Experiment Video

Updated: Jun 11, 2026

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions
06:50

Computational Prediction of Amino Acid Preferences of Potentially Multispecific Peptide-Binding Domains Involved in Protein-Protein Interactions

Published on: January 26, 2024

SH2 domains recognize contextual peptide sequence information to determine selectivity.

Bernard A Liu1, Karl Jablonowski, Eshana E Shah

  • 1Ben May Department for Cancer Research and Committee on Cancer Biology, The University of Chicago, Chicago, Illinois 60637, USA.

Molecular & Cellular Proteomics : MCP
|July 15, 2010
PubMed
Summary

Src homology 2 (SH2) domains exhibit remarkable selectivity in recognizing phosphotyrosine peptides. Their binding specificity is determined by local sequence context, including permissive and non-permissive amino acid residues.

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Published on: October 15, 2021

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Signaling

Background:

  • Protein interaction domains, such as Src homology 2 (SH2) domains, are crucial for specificity in cellular signaling pathways.
  • SH2 domains bind to phosphorylated tyrosine residues on proteins, mediating downstream signaling events initiated by tyrosine kinases.
  • Understanding SH2 domain selectivity is fundamental to deciphering phosphotyrosine signaling networks.

Purpose of the Study:

  • To investigate the selectivity of SH2 domains in recognizing diverse phosphotyrosine peptide ligands.
  • To elucidate the mechanisms underlying SH2 domain binding specificity.
  • To assess the impact of local sequence context on SH2 domain-ligand interactions.

Main Methods:

  • Examined interactions between 50 different SH2 domains and 192 phosphotyrosine peptides.
  • Peptides represented physiological motifs from FGF, insulin, and IGF-1 receptor pathways.
  • Analyzed binding data to identify determinants of SH2 domain selectivity.

Main Results:

  • Individual SH2 domains display distinct recognition properties and high selectivity for specific peptide motifs.
  • Selectivity extends beyond previously known binding motifs, influenced by both enhancing and inhibitory neighboring amino acid residues.
  • Local sequence context significantly impacts SH2 domain binding affinity and specificity.

Conclusions:

  • SH2 domain selectivity is governed by a complex interplay of local amino acid residues surrounding the phosphotyrosine site.
  • This contextual dependence increases the information content of peptide ligands, enabling precise molecular recognition.
  • The findings provide a broader paradigm for ligand recognition by protein interaction domains in physiological signaling.