1ESX

1H, 15N AND 13C STRUCTURE OF THE HIV-1 REGULATORY PROTEIN VPR : COMPARISON WITH THE N-AND C-TERMINAL DOMAIN STRUCTURE, (1-51)VPR AND (52-96)VPR

1ESX の概要

• エントリーDOI: 10.2210/pdb1esx/pdb
• 分子名称: VPR PROTEIN (1 entity in total)
• 機能のキーワード: helix, amphipatic, turn, viral protein
• 細胞内の位置: Virion: Q73369
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11411.91

構造登録者

Wecker, K.,Morellet, N.,Bouaziz, S.,Roques, B. (登録日: 2000-04-11, 公開日: 2001-04-11, 最終更新日: 2024-05-01)

主引用文献

Wecker, K.,Morellet, N.,Bouaziz, S.,Roques, B.P.
NMR structure of the HIV-1 regulatory protein Vpr in H2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains.
Eur.J.Biochem., 269:3779-3788, 2002

PubMed Abstract: The human immunodeficiency virus type 1, HIV-1, genome encodes a highly conserved regulatory gene product, Vpr (96 amino acids), which is incorporated into virions in quantities equivalent to those of the viral Gag protein. In infected cells, Vpr is believed to function during the early stages of HIV-1 replication (such as transcription of the proviral genome and migration of preintegration nuclear complex), blocks cells in G2 phase and triggers apoptosis. Vpr also plays a critical role in long-term AIDS disease by inducing viral infection in nondividing cells such as monocytes and macrophages. To gain deeper insight of the structure-function relationship of Vpr, the intact protein (residues 1-96) was synthesized. Its three-dimensional structure was analysed using circular dichroism and two-dimensional 1H- and 15N-NMR and refined by restrained molecular dynamics. In addition, 15N relaxation parameters (T1, T2) and heteronuclear 1H-15N NOEs were measured. The structure of the protein is characterized by a well-defined gamma turn(14-16)-alpha helix(17-33)-turn(34-36), followed by a alpha helix(40-48)-loop(49-54)-alpha helix(55-83) domain and ends with a very flexible C-terminal sequence. This structural determination of the whole intact Vpr molecule provide insights into the biological role played by this protein during the virus life cycle, as such amphipathic helices are believed to be involved in protein-lipid bilayers, protein-protein and/or protein-nucleic acid interactions.

PubMed: 12153575
DOI: 10.1046/j.1432-1033.2002.03067.x

実験手法

SOLUTION NMR