Journal article
Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function
Immunity (Cambridge, Mass.), v 35(4), pp 514-525
28 Oct 2011
PMID: 21962493
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Human myxovirus resistance protein 1 (MxA) is an interferon-induced dynamin-like GTPase that acts as a cell-autonomous host restriction factor against many viral pathogens including influenza viruses. To study the molecular principles of its antiviral activity, we determined the crystal structure of nucleotide-free MxA, which showed an extended three-domain architecture. The central bundle signaling element (BSE) connected the amino-terminal GTPase domain with the stalk via two hinge regions. MxA oligomerized in the crystal via the stalk and the BSE, which in turn interacted with the stalk of the neighboring monomer. We demonstrated that the intra- and intermolecular domain interplay between the BSE and stalk was essential for oligomerization and the antiviral function of MxA. Based on these results, we propose a structural model for the mechano-chemical coupling in ring-like MxA oligomers as the principle mechanism for this unique antiviral effector protein.
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► Crystal structure of antiviral dynamin-like MxA in the oligomerized state ► The hinge between BSE and stalk is crucial for MxA function ► Intermolecular BSE-stalk interface mediates oligomerization and antiviral activity ► Model of MxA rings suggests a structural mechanism for its antiviral function
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Details
- Title
- Structure of Myxovirus Resistance Protein A Reveals Intra- and Intermolecular Domain Interactions Required for the Antiviral Function
- Creators
- Song Gao - Freie Universität BerlinAlexander von der Malsburg - University of FreiburgAlexej Dick - Max Delbrück CenterKatja Faelber - Max Delbrück CenterGunnar F. Schröder - Forschungszentrum JülichOtto Haller - University of FreiburgGeorg Kochs - University of FreiburgOliver Daumke - Max Delbrück Center
- Publication Details
- Immunity (Cambridge, Mass.), v 35(4), pp 514-525
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:000296657700011
- Scopus ID
- 2-s2.0-80755153638
- Other Identifier
- 991021229982904721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Immunology