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Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.

ABSTRACT: The interferon-inducible MxA GTPase is a key mediator of cell-autonomous innate immunity against a broad range of viruses such as influenza and bunyaviruses. MxA shares a similar domain structure with the dynamin superfamily of mechanochemical enzymes, including an N-terminal GTPase domain, a central middle domain, and a C-terminal GTPase effector domain. Recently, crystal structures of a GTPase domain dimer of dynamin 1 and of the oligomerized stalk of MxA (built by the middle and GTPase effector domains) were determined. These data provide exciting insights into the architecture and antiviral function of the MxA oligomer. Moreover, the structural knowledge paves the way for the development of novel antiviral drugs against influenza and other highly pathogenic viruses.

SUBMITTER: Haller O

PROVIDER: S-EPMC2937866 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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Dynamin-like MxA GTPase: structural insights into oligomerization and implications for antiviral activity.

Haller Otto O Gao Song S von der Malsburg Alexander A Daumke Oliver O Kochs Georg G

The Journal of biological chemistry 20100610 37

The interferon-inducible MxA GTPase is a key mediator of cell-autonomous innate immunity against a broad range of viruses such as influenza and bunyaviruses. MxA shares a similar domain structure with the dynamin superfamily of mechanochemical enzymes, including an N-terminal GTPase domain, a central middle domain, and a C-terminal GTPase effector domain. Recently, crystal structures of a GTPase domain dimer of dynamin 1 and of the oligomerized stalk of MxA (built by the middle and GTPase effect ...[more]

PMID: 20538602

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