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Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus.

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-...

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Publication status:
Published

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Publisher copy:
10.1016/j.str.2013.10.013

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
Role:
Author
Journal:
Structure (London, England : 1993)
Volume:
22
Issue:
1
Pages:
136-148
Publication date:
2014-01-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:c6e9a4cc-6cf4-49ca-9102-f055ac480e36
Source identifiers:
441339
Local pid:
pubs:441339

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