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

B Xiao1, S J Smerdon, D H Jones

  • 1Division of Protein Structure, National Institute for Medical Research, Mill Hill, London, UK.

Nature
|July 13, 1995
PubMed

Insights

Researchers determined the crystal structure of the human T-cell 14-3-3 tau dimer. This structure reveals a unique channel crucial for protein interactions, including binding to protein kinase C.

Area of Science:

  • Structural biology
  • Molecular biology
  • Biochemistry

Background:

  • 14-3-3 proteins are ubiquitous and involved in diverse cellular functions.
  • These proteins play critical roles in signal transduction, exocytosis, and cell cycle regulation.

Purpose of the Study:

  • To determine the crystal structure of the human T-cell 14-3-3 tau isoform dimer.
  • To elucidate the structural basis for 14-3-3 protein function and interactions.

Main Methods:

  • X-ray crystallography was used to obtain the structure.
  • The structure was determined at a resolution of 2.6 Å.

Main Results:

  • The human T-cell 14-3-3 tau dimer structure was resolved.
  • Each monomer consists of nine antiparallel alpha-helices forming two structural domains.
  • A large, negatively charged channel is formed by the dimer, with invariant residues lining its interior.

Conclusions:

  • The determined structure provides insights into the molecular mechanisms of 14-3-3 proteins.
  • The channel structure is implicated in the binding of 14-3-3 to protein kinase C.
  • This structural information is vital for understanding signal transduction pathways involving 14-3-3 proteins.

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