Related Experiment Video

Updated: May 28, 2026

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis
08:55

Characterization of Multi-subunit Protein Complexes of Human MxA Using Non-denaturing Polyacrylamide Gel-electrophoresis

Published on: October 28, 2016

Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the

Song Gao1, Alexander von der Malsburg, Alexej Dick

  • 1Max-Delbrück-Centrum for Molecular Medicine, Crystallography, Robert-Rössle-Strasse 10, 13125 Berlin, Germany. song.gao@mdc-berlin.de

Immunity
|October 4, 2011
PubMed

Insights

Human myxovirus resistance protein 1 (MxA), an interferon-induced GTPase, restricts viral infections. Its crystal structure reveals an extended architecture essential for oligomerization and antiviral function.

Area of Science:

  • Structural biology
  • Virology
  • Immunology

Background:

  • Human myxovirus resistance protein 1 (MxA) is an interferon-induced GTPase.
  • MxA functions as a cell-autonomous host restriction factor against viral pathogens, including influenza viruses.

Purpose of the Study:

  • To elucidate the molecular principles underlying MxA's antiviral activity.
  • To determine the crystal structure of nucleotide-free MxA.

Main Methods:

  • X-ray crystallography to determine the structure of nucleotide-free MxA.
  • Analysis of domain architecture and oligomerization interfaces.

Main Results:

  • MxA exhibits an extended three-domain architecture with a central bundle signaling element (BSE) connecting the GTPase domain and stalk.
  • MxA oligomerizes via the stalk and BSE, with intermolecular interactions between neighboring monomers.
  • Intra- and intermolecular interplay between the BSE and stalk is crucial for MxA oligomerization and antiviral function.

Conclusions:

  • A structural model for mechano-chemical coupling in ring-like MxA oligomers is proposed.
  • This mechanism explains the function of MxA as an antiviral effector protein.

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