2N29

Solution-state NMR structure of Vpu cytoplasmic domain

2N29 の概要

• エントリーDOI: 10.2210/pdb2n29/pdb
• 関連するPDBエントリー: 2N28
• NMR情報: BMRB: 25592
• 分子名称: Protein Vpu (1 entity in total)
• 機能のキーワード: alpha helix, viral protein
• 由来する生物種: Human immunodeficiency virus 1 (HIV-1)
• 細胞内の位置: Host membrane ; Single-pass type I membrane protein : P69700
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6265.96

構造登録者

Zhang, H.,Lin, E.C.,Tian, Y.,Das, B.B.,Opella, S.J. (登録日: 2015-05-01, 公開日: 2015-09-30, 最終更新日: 2024-05-01)

主引用文献

Zhang, H.,Lin, E.C.,Das, B.B.,Tian, Y.,Opella, S.J.
Structural determination of virus protein U from HIV-1 by NMR in membrane environments.
Biochim.Biophys.Acta, 1848:3007-3018, 2015

PubMed Abstract: Virus protein U (Vpu) from HIV-1, a small membrane protein composed of a transmembrane helical domain and two α-helices in an amphipathic cytoplasmic domain, down modulates several cellular proteins, including CD4, BST-2/CD317/tetherin, NTB-A, and CCR7. The interactions of Vpu with these proteins interfere with the immune system and enhance the release of newly synthesized virus particles. It is essential to characterize the structure and dynamics of Vpu in order to understand the mechanisms of the protein-protein interactions, and potentially to discover antiviral drugs. In this article, we describe investigations of the cytoplasmic domain of Vpu as well as full-length Vpu by NMR spectroscopy. These studies are complementary to earlier analysis of the transmembrane domain of Vpu. The results suggest that the two helices in the cytoplasmic domain form a U-shape. The length of the inter-helical loop in the cytoplasmic domain and the orientation of the third helix vary with the lipid composition, which demonstrate that the C-terminal helix is relatively flexible, providing accessibility for interaction partners.

PubMed: 26362058
DOI: 10.1016/j.bbamem.2015.09.008

実験手法

SOLUTION NMR