A 3D-RISM/RISM study of the oseltamivir binding efficiency with the wild-type and resistance-associated mutant forms of the viral influenza B neuraminidase

• Main Authors: Phanich J., Rungrotmongkol T., Sindhikara D., Phongphanphanee S., Yoshida N., Hirata F., Kungwan N., Hannongbua S.
• Format: Journal
• Published: 2017
• Online Access: https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84959225426&origin=inward; http://cmuir.cmu.ac.th/jspui/handle/6653943832/42649
• Institution: Chiang Mai University

© 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...