Computational Simulations of HIV-1 Proteases   :   Multi-drug Resistance due to Non-active Site Mutation L90M 

作成者 Ode, Hirotaka, Neya, Saburo, Hata, Masayuki, Sugiura, Wataru, Hoshino, Tyuji
作成者の別表記 星野, 忠次
キーワード等 HIV-1, Drug Resistance, Mutation, Simulation, Inhibitors
日本十進分類法 (NDC) 490
内容 Human immunodeficiency virus type 1 (HIV-1) proliferates under the assistance of its own aspartic protease, so-called HIV-1 protease (PR), in its life cycle1. HIV-1 PR is an enzyme composed of two identical polypeptides, each of which consists of 99 amino acid residues (Fig.1A), and has a function to process the viral Gag and Gag-Pol polyprotein precursors. Because this processing is essential for the viral maturation, the inhibition of PR function leads to an incomplete viral replication and prevents the infection of other cells2. Therefore, HIV-1 PR is an attractive target for anti-HIV-1 drugs. Seven PR inhibitors (PIs) have been approved by the FDA3-9 and have successfully lowered the death rate due to acquired immune deficiency syndrome (AIDS) in advanced countries during the past decade. However, the emergence of PIresistantmutants has become a serious problem in AIDS therapies10-13. The accumulation of multi-drug-resistant mutations within HIV-1 PR makes it difficult to control viral replication in patients. Hence, PIs that maintain drug efficacy even for drug-resistant mutants are needed.
コンテンツの種類 プレプリント Preprint
ファイル形式 application/pdf
掲載誌情報 Journal of the Americal Chemical Society Vol.128 no.24 page.7887-7895 (20060621)
言語 英語
著者版フラグ author

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