6VRG
Structure of HIV-1 integrase with native amino-terminal sequence
6VRG の概要
エントリーDOI | 10.2210/pdb6vrg/pdb |
分子名称 | Integrase, ZINC ION, POTASSIUM ION, ... (5 entities in total) |
機能のキーワード | integrase, zinc ion binding, nucleic acid binding, dna integration, viral protein |
由来する生物種 | Human immunodeficiency virus 1 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 94075.87 |
構造登録者 | Eilers, G.,Gupta, K.,Allen, A.,Zhou, J.,Hwang, Y.,Cory, M.,Bushman, F.D.,Van Duyne, G.D. (登録日: 2020-02-07, 公開日: 2020-09-09, 最終更新日: 2023-10-11) |
主引用文献 | Eilers, G.,Gupta, K.,Allen, A.,Zhou, J.,Hwang, Y.,Cory, M.B.,Bushman, F.D.,Van Duyne, G. Influence of the amino-terminal sequence on the structure and function of HIV integrase. Retrovirology, 17:28-28, 2020 Cited by PubMed Abstract: Antiretroviral therapy (ART) can mitigate the morbidity and mortality caused by the human immunodeficiency virus (HIV). Successful development of ART can be accelerated by accurate structural and biochemical data on targets and their responses to inhibitors. One important ART target, HIV integrase (IN), has historically been studied in vitro in a modified form adapted to bacterial overexpression, with a methionine or a longer fusion protein sequence at the N-terminus. In contrast, IN present in viral particles is produced by proteolytic cleavage of the Pol polyprotein, which leaves a phenylalanine at the N-terminus (IN 1F). Inspection of available structures suggested that added residues on the N-terminus might disrupt proper protein folding and formation of multimeric complexes. PubMed: 32867805DOI: 10.1186/s12977-020-00537-x 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.4 Å) |
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