Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/15072
ชื่อเรื่อง: Binding energy analysis for wild-type and Y181C mutant HIV-1 RT/8-Cl TIBO complex structures: Quantum chemical calculations based on the ONIOM method
ผู้แต่ง: Saen-Oon S.
Kuno H.
Hannongbua S.
Keywords: 4,5,6,7 tetrahydroimidazo 8 chloro 5 methyl (3 methyl 2 butenyl)imidazo
RNA directed DNA polymerase
RNA directed DNA polymerase inhibitor
unclassified drug
analytic method
article
binding affinity
calculation
comparative study
complex formation
drug binding site
drug protein binding
energy
Human immunodeficiency virus 1
molecular stability
mutation
nonhuman
priority journal
quantum chemistry
wild type
Amino Acid Substitution
Dimerization
HIV-1
Kinetics
Models, Molecular
Polymorphism, Single Nucleotide
Protein Structure, Secondary
Protein Subunits
Quantum Theory
Recombinant Proteins
Reverse Transcriptase Inhibitors
RNA-Directed DNA Polymerase
Thermodynamics
Human immunodeficiency virus
Human immunodeficiency virus 1
วันที่เผยแพร่: 2005
บทคัดย่อ: Two-layered and three-layered ONIOM calculations were performed to compare the binding energies of 8-Cl TIBO inhibitor when bound into the human immunodeficiency virus reverse transcriptase binding pocket and a Y181C variant. Both consisted of 20 residues within a radius of 15 Å. A combination of different methods [HP2/6-31G(d), B3LYP/6-31G(d,p), and PM3] were performed to take advantage of ONIOM's layering strategy analysis. The obtained results clearly indicate that the Y181C mutation reduces the binding affinity and stability of the inhibitor by approximately 8-9 kcal/mol as obtained from different combined MO:MO methods. Analyses regarding the energetic components of the interaction and deformation energies for 8-Cl TIBO inhibitor upon binding were also examined extensively. Additional calculations involving the interaction energies between 8-Cl TIBO with individual residues surrounding the binding pocket were performed at MP2/6-31G(d,p) and B3LYP/6-31G(d,p) levels of theory to gain more insight into the energetic differences of wild-type and Y181C mutant type at the atomistic level. © 2005 Wiley-Liss, Inc.
URI: https://ir.swu.ac.th/jspui/handle/123456789/15072
https://www.scopus.com/inward/record.uri?eid=2-s2.0-28644442414&doi=10.1002%2fprot.20690&partnerID=40&md5=bdfa20e816813bf3ae48971687134dd4
ISSN: 8873585
Appears in Collections:Scopus 1983-2021

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