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Biomol NMR Assign. 2015 Oct;9(2):223-7. doi: 10.1007/s12104-014-9579-6. Epub 2014 Oct 10.

Solid-state NMR resonance assignments of the filament-forming CARD domain of the innate immunity signaling protein MAVS.

Author information

1
Laboratory of Macromolecular Interactions, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124, Braunschweig, Germany.
2
Laboratory of Macromolecular Interactions, Helmholtz Centre for Infection Research, Inhoffenstrasse 7, 38124, Braunschweig, Germany. christiane.ritter@helmholtz-hzi.de.

Abstract

The mitochondrial antiviral signalling protein (MAVS) is a central signal transduction hub in the innate immune response against viral infections. Viral RNA present in the cytoplasm is detected by retinoic acid inducible gene I like receptors, which then activate MAVS via heterotypic interactions between their respective caspase activation and recruitment domains (CARD). This leads to the formation of active, high molecular weight MAVS complexes formed by homotypic interactions between the single N-terminal CARDs of MAVS. Filaments formed by the N-terminal MAVS(CARD) alone are sufficient to induce the autocatalytic conversion from a monomeric to an aggregated state in a prion-like manner. Here, we present the nearly complete spectroscopic (13)C and (15)N resonance assignments of human MAVS(CARD) filaments obtained from a single sample by magic angle spinning solid-state NMR spectroscopy. The corresponding secondary chemical shifts suggest that the filamentous form of MAVS(CARD) retains an exclusively alpha-helical fold that is very similar to the X-ray structure determined previously from monomeric MAVS(CARD)-maltose binding protein fusion constructs.

KEYWORDS:

Assignments; CARD; Fibrils; MAVS; Secondary structure; Solid-state NMR

PMID:
25301530
DOI:
10.1007/s12104-014-9579-6
[Indexed for MEDLINE]

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