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Solution structure of the human Grb14-SH2 domain and comparison with the structures of the human Grb7-SH2/erbB2

Paul J Scharf1, Jill Witney, Roger Daly

  • 1Department of Biochemistry, College of Medicine, University of Vermont, Burlington, Vermont 05405, USA.

Protein Science : a Publication of the Protein Society
|August 24, 2004
PubMed

Insights

Growth factor receptor-bound protein 14 (Grb14) is overexpressed in cancers. Researchers determined the human Grb14-Src homology 2 (SH2) domain structure, aiding in understanding its role in cancer signaling.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Grb14 is an adapter protein overexpressed in estrogen receptor-positive breast and prostate cancers.
  • Grb14 modulates signals from activated receptor tyrosine kinases (RTKs) like IR, FGFR, PDGFR, and Tek/Tie2.
  • Grb14 belongs to the Grb7 family, including Grb7 and Grb10.

Purpose of the Study:

  • To determine the solution structure of the human Grb14-SH2 domain.
  • To compare the Grb14-SH2 domain structure with those of Grb7-SH2 and Grb10-SH2.

Main Methods:

  • Solution structure determination of the human Grb14-SH2 domain.
  • Structural comparison with homologous Grb7-SH2 and Grb10-SH2 domains.

Main Results:

  • The solution structure of the human Grb14-SH2 domain was solved.
  • Structural comparisons with Grb7-SH2 and Grb10-SH2 were performed.

Conclusions:

  • The determined structure provides insights into Grb14's function.
  • Structural data may aid in understanding Grb14's role in cancer signaling pathways.

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