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¹H, ¹³C and ¹⁵N assignment of D2 domain of human fibroblast growth factor receptor 4

Bettina Elshorst1, Krishna Saxena, Ulrich Schieborr

  • 1Institute for Organic Chemistry and Chemical Biology, Center for Biomolecular Magnetic Resonance, Johann Wolfgang Goethe-University Frankfurt, Max-von-Laue-Str. 7, 60438 Frankfurt, Germany.

Biomolecular NMR Assignments
|July 4, 2012
PubMed

Insights

Fibroblast growth factor receptor 4 (FGFR4) is a cancer target. Researchers assigned protein resonance for the FGFR4 D2 domain, aiding future therapeutic development.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Cancer Research

Background:

  • Fibroblast growth factor receptor 4 (FGFR4) is implicated in the progression of various cancers, including melanoma, breast, head and neck, and hepatocellular carcinoma.
  • FGFR4 represents a promising target for therapeutic interventions due to its role in cancer progression.
  • The extracellular D2 domain of FGFR4 is crucial for interactions with fibroblast growth factor and contains a heparin-binding site.

Purpose of the Study:

  • To determine the three-dimensional structure of the D2 domain of human FGFR4.
  • To provide foundational data for understanding FGFR4's role in cancer.
  • To facilitate the design of targeted therapies against FGFR4.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was employed to study the D2 domain of human FGFR4.
  • Sequential backbone and side chain resonance assignments were performed.
  • Structural and dynamic information was obtained through NMR data analysis.

Main Results:

  • Complete sequential backbone and side chain resonance assignments for the D2 domain of human FGFR4 were achieved.
  • This provides a critical step towards understanding the structural and functional properties of the FGFR4 D2 domain.
  • The assigned resonances serve as a basis for further structural and mechanistic studies.

Conclusions:

  • The successful resonance assignment of the FGFR4 D2 domain is a significant advancement for structural biology.
  • This work lays the groundwork for future investigations into FGFR4's interactions and its role in cancer.
  • The obtained data will aid in the development of novel therapeutic strategies targeting FGFR4.

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