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dc.contributor.authorJiraphorn Phanichen_US
dc.contributor.authorThanyada Rungrotmongkolen_US
dc.contributor.authorDaniel Sindhikaraen_US
dc.contributor.authorSaree Phongphanphaneeen_US
dc.contributor.authorNorio Yoshidaen_US
dc.contributor.authorFumio Hirataen_US
dc.contributor.authorNawee Kungwanen_US
dc.contributor.authorSupot Hannongbuaen_US
dc.description.abstract© 2015 The Protein Society. The binding affinity of oseltamivir to the influenza B neuraminidase and to its variants with three single substitutions, E119G, R152K, and D198N, is investigated by the MM/3D-RISM method. The binding affinity or the binding free energy of ligand to receptor was found to be determined by a subtle balance of two major contributions that largely cancel out each other: the ligand-receptor interactions and the dehydration free energy. The theoretical results of the binding affinity of the drug to the mutants reproduced the observed trend in the resistivity, measured by IC50; the high-level resistance of E119G and R152K, and the low-level resistance of D198N. For E119G and R152K, reduction of the direct drug-target interaction, especially at the mutated residue, is the main source of high-level oseltamivir resistance. This phenomenon, however, is not found in the D198N strain, which is located in the framework of the active-site.en_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleA 3D-RISM/RISM study of the oseltamivir binding efficiency with the wild-type and resistance-associated mutant forms of the viral influenza B neuraminidaseen_US
article.title.sourcetitleProtein Scienceen_US
article.volume25en_US Universityen_USödinger, Inc.en_US Universityen_US Universityen_US University, Biwako-Kusatsuen_US Mai Universityen_US
Appears in Collections:CMUL: Journal Articles

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