Particular interaction between efavirenz and the HIV-1 reverse transcriptase binding site as explained by the ONIOM2 method

被引：23
|
作者：
Nunrium, P
Kuno, M
Saen-Oon, S
Hannongbua, S
机构：
[1] Kasetsart Univ, Fac Sci, Dept Chem, Bangkok 10900, Thailand
[2] Srinakharinwirot Univ, Dept Chem, Bangkok 10330, Thailand
[3] Chulalongkorn Univ, Dept Chem, Computat Chem Unit Cell, Bangkok 10330, Thailand
来源：
CHEMICAL PHYSICS LETTERS | 2005年 / 405卷 / 1-3期
关键词：
D O I：
10.1016/j.cplett.2005.02.023
中图分类号：
O64 [物理化学（理论化学）、化学物理学];
学科分类号：
070304 ; 081704 ;
摘要：
Particular interaction between efavirenz and the HIV-1 reverse transcriptase binding site was investigated, based on the B3LYP/ 6-31G(d,p) and ONIOM2 methods. The interaction between efavirenz and Lys101 was found to be the strongest interaction, typically, -11.29 kcal/mol. The stability of this complex system leads to the foundation of the estimated binding energy of approximately -22.66 kcal/mol. Moreover, two hydrogen bonds between benzoxazin-2-one, and the backbone carbonyl oxygen and the backbone amino hydrogen of Lys101 were observed. These hydrogen bond interactions play an important role in the bound efavirenz/HIV-1 RT complex. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码：198 / 202
页数：5
相关论文
共 50 条
  • [41] Impact of residues in the nonnucleoside reverse transcriptase inhibitor binding pocket on HIV-1 reverse transcriptase heterodimer stability
    Figueiredo, Anna
    Zelina, Shannon
    Sluis-Cremer, Nicolas
    Tachedjian, Gilda
    CURRENT HIV RESEARCH, 2008, 6 (02) : 130 - 137
  • [42] Linear interaction energy approximation for binding affinities of nevirapine and HEPT analogues with HIV-1 reverse transcriptase
    Tavlarakis, Antonios
    Zhou, Ruhong
    MOLECULAR SIMULATION, 2009, 35 (15) : 1224 - 1241
  • [43] Molecular and Crystal Structure of Efavirenz, a Potent and Specific Inhibitor of HIV-1 Reverse Transcriptase, and Its Monohydrate
    Ravikumar, Krishnan
    Sridhar, Balasubramanian
    MOLECULAR CRYSTALS AND LIQUID CRYSTALS, 2009, 515 : 190 - 198
  • [44] Flexible docking of pyridinone derivatives into the non-nucleoside inhibitor binding site of HIV-1 reverse transcriptase
    Medina-Franco, JL
    Rodríguez-Morales, S
    Juárez-Gordiano, C
    Hernández-Campos, A
    Jiménez-Barbero, J
    Castillo, R
    BIOORGANIC & MEDICINAL CHEMISTRY, 2004, 12 (23) : 6085 - 6095
  • [45] A NOVEL DIPYRIDODIAZEPINONE INHIBITOR OF HIV-1 REVERSE-TRANSCRIPTASE ACTS THROUGH A NONSUBSTRATE BINDING-SITE
    WU, JC
    WARREN, TC
    ADAMS, J
    PROUDFOOT, J
    SKILES, J
    RAGHAVAN, P
    PERRY, C
    POTOCKI, I
    FARINA, PR
    GROB, PM
    BIOCHEMISTRY, 1991, 30 (08) : 2022 - 2026
  • [46] IDENTIFICATION OF THE NUCLEOTIDE-BINDING SITE OF HIV-1 REVERSE-TRANSCRIPTASE USING DTTP AS A PHOTOAFFINITY LABEL
    CHENG, N
    MERRILL, BM
    PAINTER, GR
    FRICK, LW
    FURMAN, PA
    BIOCHEMISTRY, 1993, 32 (30) : 7630 - 7634
  • [47] Convenient route to efavirenz analogues as potential non-nucleoside HIV-1 reverse transcriptase inhibitors
    Hamed, AA
    ZEITSCHRIFT FUR NATURFORSCHUNG SECTION B-A JOURNAL OF CHEMICAL SCIENCES, 2004, 59 (05): : 589 - 596
  • [48] Identification of "dual-site"-binding diarylpyrimidines targeting both NNIBP and the NNRTI adjacent site of the HIV-1 reverse transcriptase
    Feng, Da
    Zuo, Xiaofang
    Zhao, Fabao
    Lin, Hao
    Dai, Jiaojiao
    Sun, Yangyin
    De Clercq, Erik
    Pannecouque, Christophe
    Kang, Dongwei
    Liu, Xinyong
    Zhan, Peng
    EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 2023, 247
  • [49] Efavirenz accelerates HIV-1 reverse transcriptase ribonuclease h cleavage, leading to diminished zidovudine excision
    Radzio, Jessica
    Sluis-Cremer, Nicolas
    MOLECULAR PHARMACOLOGY, 2008, 73 (02) : 601 - 606
  • [50] Efavirenz enhances the proteolytic processing of an HIV-1 pol polyprotein precursor and reverse transcriptase homodimer formation
    Tachedjian, G
    Moore, KL
    Goff, SP
    Sluis-Cremer, N
    FEBS LETTERS, 2005, 579 (02): : 379 - 384
12345