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G protein mechanisms: insights from structural analysis

S R Sprang1

  • 1Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, Dallas 75235-9050, USA. sprang@howie.swmed.edu

Annual Review of Biochemistry
|January 1, 1997
PubMed
Summary

This review explores the structures and mechanisms of guanine nucleotide-binding proteins (G proteins), revealing how their conformations change upon GTP hydrolysis. Understanding these molecular switches is key to deciphering cellular signaling pathways.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Guanine nucleotide-binding proteins (G proteins) form a superfamily regulating diverse cellular processes.
  • Members like Ras, translation factors, and heterotrimeric G proteins share structural and sequence similarities, indicating a common evolutionary origin.
  • Their function relies on the hydrolysis of guanosine triphosphate (GTP) to guanosine diphosphate (GDP).

Purpose of the Study:

  • To review the structures and mechanisms of the G protein superfamily.
  • To elucidate the structural basis for GTP hydrolysis and nucleotide exchange.
  • To compare the mechanisms of various G protein regulators.

Main Methods:

  • Comparative structural analysis of G protein superfamily members.

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  • Integration of structural data with existing biochemical findings.
  • Examination of GTP- and GDP-bound conformations.

    • Main Results:

    • G proteins share a common structural core and evolutionary origin.
    • GTP hydrolysis involves specific interactions stabilizing effector-binding sites, which collapse upon GDP release.
    • GTPase-activating proteins likely stabilize transition states and may provide catalytic residues.
    • Nucleotide-release inhibitors and release factors bind to switch regions, modulating nucleotide-bound states.

    Conclusions:

    • Structural comparisons reveal conserved mechanisms within the G protein superfamily.
    • The conformational changes driven by GTP hydrolysis are central to G protein function.
    • Regulators like GTPase-activating proteins and release factors utilize specific interactions to control nucleotide binding and release.