Structure of a 14-3-3 protein and implications for coordination of multiple signalling pathways

Nature. 1995 Jul 13;376(6536):188-91. doi: 10.1038/376188a0.


A broad range of organisms and tissues contain 14-3-3 proteins, which have been associated with many diverse functions including critical roles in signal transduction pathways, exocytosis and cell cycle regulation. We report here the crystal structure of the human T-cell 14-3-3 isoform (tau) dimer at 2.6 A resolution. Each monomer (Mr 28K) is composed of an unusual arrangement of nine antiparallel alpha-helices organized as two structural domains. The dimer creates a large, negatively charged channel approximately 35 A broad, 35 A wide and 20 A deep. Overall, invariant residues line the interior of this channel whereas the more variable residues are distributed on the outer surface. At the base of this channel is a 16-residue segment of 14-3-3 which has been implicated in the binding of 14-3-3 to protein kinase C.

MeSH terms

  • 14-3-3 Proteins
  • Amino Acid Sequence
  • Animals
  • Computer Graphics
  • Crystallography, X-Ray
  • Escherichia coli
  • Humans
  • Molecular Sequence Data
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / metabolism
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • Signal Transduction*
  • T-Lymphocytes / chemistry
  • Tyrosine 3-Monooxygenase*


  • 14-3-3 Proteins
  • Proteins
  • Recombinant Proteins
  • Tyrosine 3-Monooxygenase