1VRU

HIGH RESOLUTION STRUCTURES OF HIV-1 RT FROM FOUR RT-INHIBITOR COMPLEXES

1VRU の概要

• エントリーDOI: 10.2210/pdb1vru/pdb
• 分子名称: HIV-1 REVERSE TRANSCRIPTASE, ALPHA-(2,6-DICHLOROPHENYL)-ALPHA-(2-ACETYL-5-METHYLANILINO)ACETAMIDE, ... (4 entities in total)
• 機能のキーワード: hiv-1 reverse transcriptase, 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): P04585 P04585
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 116345.22

構造登録者

Ren, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.,Stammers, D. (登録日: 1995-04-19, 公開日: 1996-04-03, 最終更新日: 2024-10-23)

主引用文献

Ren, J.,Esnouf, R.,Garman, E.,Somers, D.,Ross, C.,Kirby, I.,Keeling, J.,Darby, G.,Jones, Y.,Stuart, D.
High resolution structures of HIV-1 RT from four RT-inhibitor complexes.
Nat.Struct.Biol., 2:293-302, 1995

PubMed Abstract: We have determined the structures of four complexes of HIV-1 reverse transcriptase with non-nucleoside inhibitors, three fully refined at high resolution. The highest resolution structure is of the RT-nevirapine complex which has an R-factor of 0.186 and a root-mean-square bond length deviation of 0.015 A for all data to 2.2 A. The structures reveal a common mode of binding for these chemically diverse compounds. The common features of binding are largely hydrophobic interactions and arise from induced shape complementarity achieved by conformational rearrangement of the enzyme and conformational/configurational rearrangement of the compounds.

PubMed: 7540934
DOI: 10.1038/nsb0495-293

実験手法

X-RAY DIFFRACTION (2.4 Å)