Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/14449
Full metadata record
DC FieldValueLanguage
dc.contributor.authorBoonsri P.
dc.contributor.authorKuno M.
dc.contributor.authorHannongbua S.
dc.date.accessioned2021-04-05T03:34:50Z-
dc.date.available2021-04-05T03:34:50Z-
dc.date.issued2011
dc.identifier.issn20402503
dc.identifier.other2-s2.0-82455186221
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/14449-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-82455186221&doi=10.1039%2fc1md00162k&partnerID=40&md5=f5396527d4ea290686b48e2572eafa0a
dc.description.abstractTwo-layered ONIOM calculations were performed in order to compare the binding of efavirenz (EFV) to the HIV-1 RT binding pocket of both wild type (WT) and K103N enzymes. The K103N mutation reduces the binding affinity of the inhibitor by 5.81 kcal mol -1 as obtained from the ONIOM2 (B3LYP/6-31G(d,p):PM3) method. These indicate that the loss of binding energy to K103N mutation can attribute to a weakened attractive interaction between the drug and residues surrounding in the binding pocket. The deformation of the K103N binding pocket requires more energy for structural rearrangement than that of the WT by approximately 4.0 kcal mol -1. Moreover, the pairwise energies perfectly demonstrate that the K103N mutation affects on the loss of the interaction energy. In addition, the main influences are due to residues surrounding in the binding pocket; K101, K102, S105, V179, W229, P236 and E138. In particular, two residues; K101 and S105, established hydrogen bondings with the inhibitor. ONIOM calculations, resulting in the details of binding energy, interaction energy and deformation energy can be used to identify the key interaction and structural requirements of more potent HIV-1 RT inhibitor. © 2011 The Royal Society of Chemistry.
dc.subjectefavirenz
dc.subjectRNA directed DNA polymerase
dc.subjectamino acid sequence
dc.subjectarticle
dc.subjectbinding affinity
dc.subjectbinding kinetics
dc.subjectbinding site
dc.subjectdrug interaction
dc.subjectdrug protein binding
dc.subjectenergy
dc.subjectenzyme structure
dc.subjecthydrogen bond
dc.subjectmathematical analysis
dc.subjectmutant
dc.subjectpriority journal
dc.subjectwild type
dc.titleKey interactions of the mutant HIV-1 reverse transcriptase/efavirenz: An evidence obtained from ONIOM method
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationMedChemComm. Vol 2, No.12 (2011), p.1181-1187
dc.identifier.doi10.1039/c1md00162k
Appears in Collections:Scopus 1983-2021

Files in This Item:
There are no files associated with this item.


Items in SWU repository are protected by copyright, with all rights reserved, unless otherwise indicated.