2PJV

solution structure of hiv-1 gp41 fusion domain bound to DPC micelle

2PJV の概要

• エントリーDOI: 10.2210/pdb2pjv/pdb
• 分子名称: Envelope glycoprotein (1 entity in total)
• 機能のキーワード: hiv, gp41, fusion, membrane, protein, dpc, virus, viral protein
• 由来する生物種: Human immunodeficiency virus 1
• 細胞内の位置: Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P19551
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2824.35

構造登録者

Li, Y.,Tamm, L.K. (登録日: 2007-04-16, 公開日: 2007-05-01, 最終更新日: 2024-05-22)

主引用文献

Li, Y.,Tamm, L.K.
Structure and Plasticity of the Human Immunodeficiency Virus gp41 Fusion Domain in Lipid Micelles and Bilayers.
Biophys.J., 93:876-885, 2007

PubMed Abstract: A thorough understanding of the structure of fusion domains of enveloped viruses in changing lipid environments helps us to formulate mechanistic models on how they might function in mediating viral entry by membrane fusion. We have expressed the N-terminal fusion domain of HIV-1 gp41 as a construct that is water-soluble in the absence of membranes, but that also binds with high affinity to lipid micelles and bilayers in their presence. We have solved the structure and studied the dynamics of this domain bound to dodecylphosphocholine micelles by homo- and heteronuclear NMR spectroscopy. The fusion peptide forms a stable hydrophobic helix from Ile(4) to Ala(14), but is increasingly more disordered and dynamic in a segment of intermediate polarity that stretches from Ala(15) to Ser(23). When bound to lipid bilayers at low concentration, the HIV fusion domain is also largely alpha-helical, as determined by CD and FTIR spectroscopy. However, at higher protein/lipid ratios, the domain is partially converted to form beta-structures in lipid bilayers. Controlled lipid mixing occurs at concentrations that support the alpha-helical, but not the beta-strand conformation.

PubMed: 17513369
DOI: 10.1529/biophysj.106.102335

実験手法

SOLUTION NMR