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- W2005209853 abstract "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-angle X-ray scattering with MDS and ensemble analysis, we captured the structure and dynamics of M in solution. Our analysis reveals a large positively charged patch on the protein surface that is involved in membrane interaction. Structural analysis of DOPC-induced polymerization of M into helical filaments using electron microscopy leads to a model of M self-assembly. The conservation of the Ca²⁺ binding sites suggests a role for calcium in the replication and morphogenesis of pneumoviruses." @default.
- W2005209853 created "2016-06-24" @default.
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- W2005209853 date "2014-01-01" @default.
- W2005209853 modified "2023-10-14" @default.
- W2005209853 title "Structure and Self-Assembly of the Calcium Binding Matrix Protein of Human Metapneumovirus" @default.
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- W2005209853 doi "https://doi.org/10.1016/j.str.2013.10.013" @default.
- W2005209853 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3887258" @default.
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