タイトル（掲載誌）Journal of Molecular Biology
一般注記type:text
[Abstract] A prominent characteristic of human immunodeficiency virus type 1 (HIV-1) is its highgenetic variability, which generates diversity of the virus and often causes a serious problem of the emergence of drug-resistant mutants. Subtype B HIV-1 is dominant in advanced countries, and themortality rate due to subtype B HIV-1 has been decreased during the past decade. In contrast, the number of patients with non-subtype B viruses is still increasing in developing countries. One of the reasons for the prevalence of non-subtype B viruses is lack of information about the biological and therapeutic differences between subtype B and non-subtype B viruses. M36I is the most frequently observed polymorphism in non-subtype B HIV-1 proteases. However, since the 36th residue is located at a non-active site of the protease and has no direct interaction with any ligands, the structural role of M36I remains unclear. In this study, we performed molecular dynamics (MD) simulations of M36I protease incomplex with nelfinavir and revealed the influence of the M36I mutation. The results show that M36I regulates the size of the binding cavity of the protease. The reason for the rare emergence of D30N variants in non-subtype B HIV-1 proteases was also clarified from our computational analysis.
一次資料へのリンクURLhttps://opac.ll.chiba-u.jp/da/curator/900040561/JMB-D-07-00242.pdf
関連情報（DOI）10.1016/j.jmb.2007.04.081
連携機関・データベース国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）