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• W2212345909 startingPage "82" @default.
• W2212345909 abstract "Increased reports of oseltamivir (OTV)-resistant strains of the influenza virus, such as the H274Y mutation on its neuraminidase (NA), have created some cause for concern. Many studies have been conducted in the attempt to uncover the mechanism of OTV resistance in H274Y NA. However, most of the reported studies on H274Y focused only on the drug-bound system, so the direct effects of the mutation on NA itself prior to drug binding still remain unclear. Therefore, molecular dynamics simulations of NA in apo form, followed by principal component analysis and interaction energy calculations, were performed to investigate the structural changes of the NA binding site as a result of the H274Y mutation. It was observed that the disruption of the NA binding site due to the H274Y mutation was initiated by the repulsive effect of Y274 on the 250-loop, which in turn altered the hydrogen-bonding network around residue 274. The rotated W295 side chain caused the upward movement of the 340-loop. Consequently, sliding box docking results suggested that the binding pathway of OTV was compromised because of the disruption of this binding site. This study also highlighted the importance of the functional group at C6 of the sialic acid mimicry. It is hoped that these results will improve the understanding of OTV resistance and shed some light on the design of a novel anti-influenza drug." @default.
• W2212345909 created "2016-06-24" @default.
• W2212345909 creator A5008474034 @default.
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• W2212345909 date "2016-01-08" @default.
• W2212345909 modified "2023-10-16" @default.
• W2212345909 title "H274Y’s Effect on Oseltamivir Resistance: What Happens Before the Drug Enters the Binding Site" @default.
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• W2212345909 doi "https://doi.org/10.1021/acs.jcim.5b00331" @default.
• W2212345909 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26703840" @default.
• W2212345909 hasPublicationYear "2016" @default.
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