Article
Stalk domain of the dynamin-like MxA GTPase protein mediates membrane binding and liposome tubulation via the unstructured L4 loop.
The Journal of biological chemistry - 28 Oct 2011
von der Malsburg Alexander, Abutbul-Ionita Inbal, Haller Otto, Kochs Georg, Danino Dganit
Abstract excerpt
The human MxA protein is an interferon-induced large GTPase with antiviral activity against a wide range of viruses, including influenza viruses. Recent structural data demonstrated that MxA oligomerizes into multimeric filamentous or ring-like structures by virtue of its stalk domain. Here, we show that negatively charged lipid membranes support MxA self-assembly. Like dynamin, MxA assembled around spherical...
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