Three-dimensional structure of the tyrosine kinase c-Src

Nature. 1997 Feb 13;385(6617):595-602. doi: 10.1038/385595a0.


The structure of a large fragment of the c-Src tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tall, has been determined at 1.7 A resolution in a closed, inactive state. Interactions among domains, stabilized by binding of the phosphorylated tail to the SH2 domain, lock the molecule in a conformation that simultaneously disrupts the kinase active site and sequesters the binding surfaces of the SH2 and SH3 domains. The structure shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Enzyme Activation
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation*
  • Proto-Oncogene Proteins pp60(c-src) / chemistry*
  • src Homology Domains


  • Proto-Oncogene Proteins pp60(c-src)

Associated data

  • PDB/1FMK