Abstract |
The crystal structure of the F protein (prefusion form) of the paramyxovirus parainfluenza virus 5 (PIV5) WR isolate was determined. We investigated the basis by which point mutations affect fusion in PIV5 isolates W3A and WR, which differ by two residues in the F ectodomain. The P22 stabilizing site acts through a local conformational change and a hydrophobic pocket interaction, whereas the S443 destabilizing site appears sensitive to both conformational effects and amino acid charge/polarity changes.
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Authors | Taylor A Poor, Albert S Song, Brett D Welch, Christopher A Kors, Theodore S Jardetzky, Robert A Lamb |
Journal | Journal of virology
(J Virol)
Vol. 89
Issue 6
Pg. 3438-41
(Mar 2015)
ISSN: 1098-5514 [Electronic] United States |
PMID | 25589638
(Publication Type: Journal Article, Research Support, N.I.H., Extramural, Research Support, Non-U.S. Gov't)
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Copyright | Copyright © 2015, American Society for Microbiology. All Rights Reserved. |
Chemical References |
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Topics |
- Amino Acid Motifs
- Crystallography, X-Ray
- Humans
- Mutation
- Parainfluenza Virus 5
(chemistry, genetics, metabolism)
- Protein Stability
- Protein Structure, Tertiary
- Rubulavirus Infections
(virology)
- Viral Fusion Proteins
(chemistry, genetics, metabolism)
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