5JYN
Structure of the transmembrane domain of HIV-1 gp41 in bicelle
Summary for 5JYN
| Entry DOI | 10.2210/pdb5jyn/pdb |
| NMR Information | BMRB: 30090 |
| Descriptor | Envelope glycoprotein gp160 (1 entity in total) |
| Functional Keywords | transmembrane domain, lipid bilayer, transmembrane trimer, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 3 |
| Total formula weight | 13951.81 |
| Authors | Dev, J.,Fu, Q.,Park, D.,Chen, B.,Chou, J.J. (deposition date: 2016-05-14, release date: 2016-06-29, Last modification date: 2024-05-15) |
| Primary citation | Dev, J.,Park, D.,Fu, Q.,Chen, J.,Ha, H.J.,Ghantous, F.,Herrmann, T.,Chang, W.,Liu, Z.,Frey, G.,Seaman, M.S.,Chen, B.,Chou, J.J. Structural basis for membrane anchoring of HIV-1 envelope spike. Science, 353:172-175, 2016 Cited by PubMed Abstract: HIV-1 envelope spike (Env) is a type I membrane protein that mediates viral entry. We used nuclear magnetic resonance to determine an atomic structure of the transmembrane (TM) domain of HIV-1 Env reconstituted in bicelles that mimic a lipid bilayer. The TM forms a well-ordered trimer that protects a conserved membrane-embedded arginine. An amino-terminal coiled-coil and a carboxyl-terminal hydrophilic core stabilize the trimer. Individual mutations of conserved residues did not disrupt the TM trimer and minimally affected membrane fusion and infectivity. Major changes in the hydrophilic core, however, altered the antibody sensitivity of Env. These results show how a TM domain anchors, stabilizes, and modulates a viral envelope spike and suggest that its influence on Env conformation is an important consideration for HIV-1 immunogen design. PubMed: 27338706DOI: 10.1126/science.aaf7066 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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