2PJV
solution structure of hiv-1 gp41 fusion domain bound to DPC micelle
Summary for 2PJV
| Entry DOI | 10.2210/pdb2pjv/pdb |
| Descriptor | Envelope glycoprotein (1 entity in total) |
| Functional Keywords | hiv, gp41, fusion, membrane, protein, dpc, virus, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Surface protein gp120: Virion membrane ; Peripheral membrane protein . Transmembrane protein gp41: Virion membrane ; Single-pass type I membrane protein : P19551 |
| Total number of polymer chains | 1 |
| Total formula weight | 2824.35 |
| Authors | Li, Y.,Tamm, L.K. (deposition date: 2007-04-16, release date: 2007-05-01, Last modification date: 2024-05-22) |
| Primary citation | 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 Cited by 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: 17513369DOI: 10.1529/biophysj.106.102335 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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