1DLO
HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
1DLO の概要
| エントリーDOI | 10.2210/pdb1dlo/pdb |
| 分子名称 | HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE (2 entities in total) |
| 機能のキーワード | nucleotidyltransferase |
| 由来する生物種 | Human immunodeficiency virus 1 詳細 |
| 細胞内の位置 | Matrix protein p17: Virion (Potential). Capsid protein p24: Virion (Potential). Nucleocapsid protein p7: Virion (Potential). Reverse transcriptase/ribonuclease H: Virion (Potential). Integrase: Virion (Potential): P03366 P03366 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 113899.63 |
| 構造登録者 | Hsiou, Y.,Ding, J.,Das, K.,Hughes, S.,Arnold, E. (登録日: 1996-04-17, 公開日: 1996-08-01, 最終更新日: 2024-02-07) |
| 主引用文献 | Hsiou, Y.,Ding, J.,Das, K.,Clark Jr., A.D.,Hughes, S.H.,Arnold, E. Structure of unliganded HIV-1 reverse transcriptase at 2.7 A resolution: implications of conformational changes for polymerization and inhibition mechanisms. Structure, 4:853-860, 1996 Cited by PubMed Abstract: HIV-1 reverse transcriptase (RT) is a major target for anti-HIV drugs. A considerable amount of information about the structure of RT is available, both unliganded and in complex with template-primer or non-nucleoside RT inhibitors (NNRTIs). But significant conformational differences in the p66 polymerase domain among the unliganded structures have complicated the interpretation of these data, leading to different proposals for the mechanisms of polymerization and inhibition. PubMed: 8805568DOI: 10.1016/S0969-2126(96)00091-3 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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