Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module

Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module

The dynamin-like MxA GTPase (Myxovirus resistance protein 1) mediates cellular resistance against a wide range of viruses. MxA is composed of an amino-terminal G domain, a middle domain and a carboxy-terminal GTPase effector domain. We recently determined the structure of the middle domain and GTPas...

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Veröffentlicht in:Small GTPases 2010-07, Vol.1 (1), p.62-64
Hauptverfasser: Daumke, Oliver, Gao, Song, von der Malsburg, Alexander, Haller, Otto, Kochs, Georg
Format: Artikel
Sprache:eng
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Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Extra View
Landes
Organogenesis
Proteins
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container_end_page 64
container_issue 1
container_start_page 62
container_title Small GTPases
container_volume 1
creator Daumke, Oliver
Gao, Song
von der Malsburg, Alexander
Haller, Otto
Kochs, Georg
description The dynamin-like MxA GTPase (Myxovirus resistance protein 1) mediates cellular resistance against a wide range of viruses. MxA is composed of an amino-terminal G domain, a middle domain and a carboxy-terminal GTPase effector domain. We recently determined the structure of the middle domain and GTPase effector domain of MxA constituting an elongated helical stalk, and elucidated the mechanism how the stalk mediates formation of ring-like MxA oligomers. Here, we shortly review our work and discuss the MxA rings as functional units of a cellular module orchestrating and executing the antiviral response.
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subjects Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Extra View
Landes
Organogenesis
Proteins
title Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module
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