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Related Experiment Videos

Do G protein subunits associate via a three-stranded coiled coil?

A N Lupas1, J M Lupas, J B Stock

  • 1Max Planck Institut für Biochemie, Martinsried, Germany.

FEBS Letters
|December 14, 1992
PubMed
Summary

Computer analysis suggests G protein trimers assemble through a three-stranded coiled-coil interaction at subunit N-termini. This study models the beta gamma N-terminal domain and alpha subunit association.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • G protein subunits (alpha, beta, gamma) mediate cellular signaling.
  • Previous studies implicated N-termini of alpha and beta subunits in G protein interactions.

Purpose of the Study:

  • To identify potential coiled-coil structures in G protein subunit N-termini.
  • To propose a structural model for beta gamma N-terminal interactions.
  • To hypothesize the mechanism of alpha subunit association with beta gamma.

Main Methods:

  • Utilized a computer-based prediction algorithm.
  • Identified probable coiled-coil segments in G protein subunit N-termini.
  • Developed a structural model for the N-terminal domain of beta gamma.

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Main Results:

  • Predicted coiled-coil segments at the N-termini of G protein alpha, beta, and gamma subunits.
  • Indicated that G protein trimers may assemble via a three-stranded coiled coil.
  • Presented a structural model for the N-terminal domain of beta gamma.

Conclusions:

  • G protein trimer formation likely involves a three-stranded coiled-coil interaction at subunit N-termini.
  • A structural model for beta gamma N-terminal domain and alpha association is proposed.
  • The reversible association of alpha to beta gamma is hypothesized.