1LWE

CRYSTAL STRUCTURE OF M41L/T215Y MUTANT HIV-1 REVERSE TRANSCRIPTASE (RTMN) IN COMPLEX WITH NEVIRAPINE

1LWE の概要

• エントリーDOI: 10.2210/pdb1lwe/pdb
• 関連するPDBエントリー: 1C0T 1C0U 1C1B 1C1C 1DTQ 1DTT 1EP4 1FK9 1FKO 1FKP 1JKH 1JLA 1JLB 1JLC 1JLE 1JLF 1JLG 1JLQ 1KLM 1LW0 1LW2 1LWC 1LWF 1REV 1RT1 1RT2 1RT3 1RT4 1RT5 1RT6 1RT7 1RTH 1RTI 1RTJ 1VRT 1VRU
• 分子名称: HIV-1 REVERSE TRANSCRIPTASE, PHOSPHATE ION, 11-CYCLOPROPYL-5,11-DIHYDRO-4-METHYL-6H-DIPYRIDO[3,2-B:2',3'-E][1,4]DIAZEPIN-6-ONE, ... (5 entities in total)
• 機能のキーワード: hiv-1 reverse transcriptase, aids, azt, 3tc, nrti, nevirapine, drug resistance mutations, transferase
• 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: 116443.33

構造登録者

Ren, J.,Chamberlain, P.P.,Nichols, C.E.,Douglas, L.,Stuart, D.I.,Stammers, D.K. (登録日: 2002-05-31, 公開日: 2002-10-30, 最終更新日: 2021-11-10)

主引用文献

Chamberlain, P.P.,Ren, J.,Nichols, C.E.,Douglas, L.,Lennerstrand, J.,Larder, B.A.,Stuart, D.I.,Stammers, D.K.
Crystal structures of Zidovudine- or Lamivudine-resistant human immunodeficiency virus type 1 reverse transcriptases containing mutations at codons 41, 184, and 215.
J.Virol., 76:10015-10019, 2002

PubMed Abstract: Six structures of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) containing combinations of resistance mutations for zidovudine (AZT) (M41L and T215Y) or lamivudine (M184V) have been determined as inhibitor complexes. Minimal conformational changes in the polymerase or nonnucleoside RT inhibitor sites compared to the mutant RTMC (D67N, K70R, T215F, and K219N) are observed, indicating that such changes may occur only with certain combinations of mutations. Model building M41L and T215Y into HIV-1 RT-DNA and docking in ATP that is utilized in the pyrophosphorolysis reaction for AZT resistance indicates that some conformational rearrangement appears necessary in RT for ATP to interact simultaneously with the M41L and T215Y mutations.

PubMed: 12208978
DOI: 10.1128/JVI.76.19.10015-10019.2002

実験手法

X-RAY DIFFRACTION (2.81 Å)