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Related Experiment Videos

Grb7-SH2 domain dimerisation is affected by a single point mutation.

Corrine J Porter1, Matthew C J Wilce, Joel P Mackay

  • 1School of Biomedical and Chemical Sciences, University of Western Australia, 35 Stirling Highway, Crawley, Perth, WA 6009, Australia.

European Biophysics Journal : EBJ
|April 21, 2005
PubMed
Summary

Growth factor receptor bound protein 7 (Grb7) is an adaptor protein implicated in breast cancer. The Grb7 Src homology 2 (SH2) domain, crucial for ErbB2 interaction, was found to be dimeric, a property that can be disrupted by specific mutations.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Growth factor receptor bound protein 7 (Grb7) is an adaptor protein.
  • Grb7 is co-overexpressed with the ErbB2 receptor in breast tumors.
  • The interaction between Grb7 and ErbB2 is mediated by the Grb7 Src homology 2 (SH2) domain.

Purpose of the Study:

  • To investigate the self-association properties of the Grb7-SH2 domain.
  • To determine if the Grb7-SH2 domain exists as a monomer or dimer.
  • To identify mutations that alter the oligomeric state of the Grb7-SH2 domain for biophysical studies.

Main Methods:

  • Sedimentation equilibrium ultracentrifugation to assess protein oligomerization.
  • Size-exclusion chromatography to analyze the effect of mutations on protein structure.

Related Experiment Videos

  • Site-directed mutagenesis to alter specific amino acid residues.

    • Main Results:

    • The Grb7-SH2 domain was confirmed to exist as a homodimer in solution.
    • A dissociation constant (Kd) of approximately 11 μM was determined for the Grb7-SH2 domain dimer.
    • Mutation of phenylalanine 511 to arginine resulted in a monomeric form of the Grb7-SH2 domain.

    Conclusions:

    • The Grb7-SH2 domain exhibits self-association, existing as a dimer.
    • Specific mutations, such as F511R, can disrupt dimerization and yield a monomeric Grb7-SH2 domain.
    • This engineered monomeric Grb7-SH2 domain is a valuable tool for future biophysical and structural investigations.