Structural biology of protein tyrosine kinases

Cell Mol Life Sci. 2006 Nov;63(22):2608-25. doi: 10.1007/s00018-006-6202-8.


Our current understanding of the structure, mechanism of action and modes of regulation of the protein tyrosine kinase family owes a great deal to structural biology. Structures are now available for more than 20 different tyrosine kinase domains, many of these in multiple conformational states. They form the basis for the design of experiments to further investigate the role of different structural elements in the normal function and regulation of the protein and in the pathogenesis of many human diseases. Once thought to be too similar to be specifically inhibited by a small molecule, structural differences between kinases allow the design of compounds which inhibit only an acceptable few. This review gives a general overview of protein tyrosine kinase structural biology, including a discussion of the strengths and limitations of the investigative methods involved.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Chemistry, Pharmaceutical
  • Crystallography, X-Ray
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Conformation
  • Protein Structure, Tertiary
  • Protein-Tyrosine Kinases / chemistry*
  • src Homology Domains


  • Protein-Tyrosine Kinases