1HMV

THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1

1HMV の概要

• エントリーDOI: 10.2210/pdb1hmv/pdb
• 分子名称: HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P66), HIV-1 REVERSE TRANSCRIPTASE (SUBUNIT P51), MAGNESIUM ION (3 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: 8
• 化学式量合計: 463649.47

構造登録者

Rodgers, D.W.,Gamblin, S.J.,Harris, B.A.,Ray, S.,Culp, J.S.,Hellmig, B.,Woolf, D.J.,Debouck, C.,Harrison, S.C. (登録日: 1994-12-15, 公開日: 1995-03-31, 最終更新日: 2024-02-07)

主引用文献

Rodgers, D.W.,Gamblin, S.J.,Harris, B.A.,Ray, S.,Culp, J.S.,Hellmig, B.,Woolf, D.J.,Debouck, C.,Harrison, S.C.
The structure of unliganded reverse transcriptase from the human immunodeficiency virus type 1.
Proc.Natl.Acad.Sci.USA, 92:1222-1226, 1995

PubMed Abstract: The crystal structure of the reverse transcriptase (RT) from the type 1 human immunodeficiency virus has been determined at 3.2-A resolution. Comparison with complexes between RT and the polymerase inhibitor Nevirapine [Kohlstaedt, L.A., Wang, J., Friedman, J.M., Rice, P.A. & Steitz, T.A. (1992) Science 256, 1783-1790] and between RT and an oligonucleotide [Jacobo-Molina, A., Ding, J., Nanni, R., Clark, A. D., Lu, X., Tantillo, C., Williams, R. L., Kamer, G., Ferris, A. L., Clark, P., Hizi, A., Hughes, S. H. & Arnold, E. (1993) Proc. Natl. Acad. Sci. USA 90, 6320-6324] reveals changes associated with ligand binding. The enzyme is a heterodimer (p66/p51), with domains labeled "fingers," "thumb," "palm," and "connection" in both subunits, and a ribonuclease H domain in the larger subunit only. The most striking difference between RT and both complex structures is the change in orientation of the p66 thumb (approximately 33 degrees rotation). Smaller shifts relative to the core of the molecule were also found in other domains, including the p66 fingers and palm, which contain the polymerase active site. Within the polymerase catalytic region itself, there are no rearrangements between RT and the RT/DNA complex. In RT/Nevirapine, the drug binds in the p66 palm near the polymerase active site, a region that is well-packed hydrophobic core in the unliganded enzyme. Room for the drug is provided by movement of a small beta-sheet within the palm domain of the Nevirapine complex. The rearrangement within the palm and thumb, as well as domain shifts relative to the enzyme core, may prevent correct placement of the oligonucleotide substrate when the drug is bound.

PubMed: 7532306
DOI: 10.1073/pnas.92.4.1222

実験手法

X-RAY DIFFRACTION (3.2 Å)