1VPU

NMR SOLUTION STRUCTURE OF THE HIV-1 VPU CYTOPLASMIC DOMAIN, 9 STRUCTURES

1VPU の概要

• エントリーDOI: 10.2210/pdb1vpu/pdb
• 分子名称: VPU PROTEIN (1 entity in total)
• 機能のキーワード: hiv, vpu, aids
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: Host membrane; Single-pass type I membrane protein (By similarity): P19554
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 5111.44

構造登録者

Willbold, D.,Hoffmann, S.,Rosch, P. (登録日: 1997-01-28, 公開日: 1997-05-15, 最終更新日: 2024-05-22)

主引用文献

Willbold, D.,Hoffmann, S.,Rosch, P.
Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.
Eur.J.Biochem., 245:581-588, 1997

PubMed Abstract: The human immunodeficiency virus type 1 Vpu protein enhances virus particle release from infected cells, decreases the tendency of syncytia formation and induces degradation of human CD4 receptor. It is known that the cytoplasmic part of Vpu is responsible for direct interaction to and degradation of CD4. The tertiary fold of the Vpu cytoplasmic domain in aqueous solution was determined employing NMR spectroscopy and molecular-dynamics simulated-annealing protocols. We found a very well defined amphipathic alpha-helix in the membrane proximal part (40-50), a less well defined helix (60-68), and a short alpha-helix at the C-terminus (75-79). We further determined the overall tertiary structure based on long-range nuclear Overhauser enhancement effects. Correlation of results from mutation experiments of Vpu and the structure data is discussed.

PubMed: 9182993
DOI: 10.1111/j.1432-1033.1997.t01-1-00581.x

実験手法

SOLUTION NMR