On the stability of parainfluenza virus 5 F proteins
Journal of virology, 2015•Am Soc Microbiol
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.
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.
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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