Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus.
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ABSTRACT:
SUBMITTER: Leyrat C
PROVIDER: S-EPMC3887258 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Publications
Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus.
Leyrat Cedric C Renner Max M Harlos Karl K Huiskonen Juha T JT Grimes Jonathan M JM
Structure (London, England : 1993) 20131205 1
The matrix protein (M) of paramyxoviruses plays a key role in determining virion morphology by directing viral assembly and budding. Here, we report the crystal structure of the human metapneumovirus M at 2.8 Å resolution in its native dimeric state. The structure reveals the presence of a high-affinity Ca²⁺ binding site. Molecular dynamics simulations (MDS) predict a secondary lower-affinity site that correlates well with data from fluorescence-based thermal shift assays. By combining small-ang ...[more]
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