- 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 Ca 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-an...
Expand abstract - Publisher copy:
- 10.1016/j.str.2013.10.013
-
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- Journal:
- Structure
- Volume:
- 22
- Issue:
- 1
- Pages:
- 136-148
- Publication date:
- 2014-01-07
- DOI:
- EISSN:
-
1878-4186
- ISSN:
-
0969-2126
- URN:
-
uuid:f09a3774-8df2-4337-b1c2-0c4cb253e9bb
- Source identifiers:
-
447224
- Local pid:
- pubs:447224
- Copyright date:
- 2014
Journal article
Structure and self-assembly of the calcium binding matrix protein of human metapneumovirus
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