Structures of Src-family tyrosine kinases

Curr Opin Struct Biol. 1997 Dec;7(6):777-85. doi: 10.1016/s0959-440x(97)80146-7.

Abstract

The crystal structures of three Src-family tyrosine kinases have been determined recently. The structure of the catalytic domain of Lck has been determined in the active autophosphorylated state. The structures of larger constructs of c-Src and Hck, containing the SH3, SH2 and catalytic domains, as well as a C-terminal regulatory tail, have been determined in the down-regulated state, phosphorylated in the C-terminal tail. A comparison of these structures leads to an unanticipated mechanism for the regulation of catalytic activity by cooperative interactions between the SH2, SH3 and catalytic domains.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • Down-Regulation / physiology
  • Hydrogen Bonding
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck) / chemistry
  • Models, Molecular
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Conformation
  • Protein-Tyrosine Kinases / chemistry
  • Proto-Oncogene Proteins / chemistry
  • Proto-Oncogene Proteins c-hck
  • Proto-Oncogene Proteins pp60(c-src) / chemistry
  • src Homology Domains
  • src-Family Kinases / chemistry*
  • src-Family Kinases / metabolism

Substances

  • Proto-Oncogene Proteins
  • Protein-Tyrosine Kinases
  • Lymphocyte Specific Protein Tyrosine Kinase p56(lck)
  • Proto-Oncogene Proteins c-hck
  • Proto-Oncogene Proteins pp60(c-src)
  • src-Family Kinases