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Protein domains are small structurally independent units that are part of a single amino acid chain.  Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
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Assessing Cellular Target Engagement by SHP2 PTPN11 Phosphatase Inhibitors
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Engineered SH2 Domains for Targeted Phosphoproteomics.

Gregory D Martyn1,2, Gianluca Veggiani1, Ulrike Kusebauch3

  • 1Donnelly Centre for Cellular and Biomolecular Research, University of Toronto, 160 College Street, Toronto, Ontario M5S3E1, Canada.

ACS Chemical Biology
|May 25, 2022
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Summary
This summary is machine-generated.

Researchers developed novel superbinder Src-Homology 2 (SH2) domains to improve phosphotyrosine (pTyr) enrichment. These engineered domains offer enhanced affinity and specificity, advancing phosphoproteome analysis for disease research.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Understanding the phosphoproteome is crucial for deciphering human disease mechanisms.
  • Current methods for enriching phosphotyrosine (pTyr) peptides have limitations in scope and applicability.

Purpose of the Study:

  • To engineer novel Src-Homology 2 (SH2) superbinder domains with enhanced affinity and specificity for phosphotyrosine (pTyr) peptides.
  • To improve the enrichment and analysis of the phosphoproteome for disease research.

Main Methods:

  • Phage display was used to select and engineer superbinder SH2 domains (e.g., superFes, sFes¹).
  • Structural and functional analyses were performed on engineered SH2 superbinder variants.
  • Mass spectrometry (MS) and affinity purification (AP) techniques were employed to assess enrichment capabilities.

Main Results:

  • Engineered SH2 superbinders (sFes¹, sSrc¹) demonstrated high affinity for pTyr-peptides.
  • Grafting superbinder motifs into other SH2 domains confirmed increased binding affinity.
  • SH2 superbinders exhibited distinct specificity profiles and superior pTyr-peptide enrichment capabilities via MS.
  • Combinations of SH2 superbinders enabled deep and broad enrichment of unique pTyr-peptide subsets.

Conclusions:

  • Novel SH2 superbinders significantly enhance the enrichment of diverse phosphotyrosine-containing peptides.
  • These engineered tools offer improved depth and coverage for phosphoproteome analysis.
  • The developed SH2 superbinders represent a valuable advancement for studying disease mechanisms at the molecular level.