6UJU
Structure of the HIV-1 gp41 transmembrane domain and cytoplasmic tail (LLP2)
Summary for 6UJU
| Entry DOI | 10.2210/pdb6uju/pdb |
| Related | 5JYN |
| NMR Information | BMRB: 30678 |
| Descriptor | Envelope glycoprotein GP41 (1 entity in total) |
| Functional Keywords | viral protein, transmembrane domain, cytoplasmic tail, lipid bilayer, membrane protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 3 |
| Total formula weight | 39117.52 |
| Authors | Piai, A.,Fu, Q.,Cai, Y.,Ghantous, F.,Xiao, T.,Shaik, M.M.,Peng, H.,Rits-Volloch, S.,Liu, Z.,Chen, W.,Seaman, M.S.,Chen, B.,Chou, J.J. (deposition date: 2019-10-03, release date: 2020-05-13, Last modification date: 2024-05-15) |
| Primary citation | Piai, A.,Fu, Q.,Cai, Y.,Ghantous, F.,Xiao, T.,Shaik, M.M.,Peng, H.,Rits-Volloch, S.,Chen, W.,Seaman, M.S.,Chen, B.,Chou, J.J. Structural basis of transmembrane coupling of the HIV-1 envelope glycoprotein. Nat Commun, 11:2317-2317, 2020 Cited by PubMed Abstract: The prefusion conformation of HIV-1 envelope protein (Env) is recognized by most broadly neutralizing antibodies (bnAbs). Studies showed that alterations of its membrane-related components, including the transmembrane domain (TMD) and cytoplasmic tail (CT), can reshape the antigenic structure of the Env ectodomain. Using nuclear magnetic resonance (NMR) spectroscopy, we determine the structure of an Env segment encompassing the TMD and a large portion of the CT in bicelles. The structure reveals that the CT folds into amphipathic helices that wrap around the C-terminal end of the TMD, thereby forming a support baseplate for the rest of Env. NMR dynamics measurements provide evidences of dynamic coupling across the TMD between the ectodomain and CT. Pseudovirus-based neutralization assays suggest that CT-TMD interaction preferentially affects antigenic structure near the apex of the Env trimer. These results explain why the CT can modulate the Env antigenic properties and may facilitate HIV-1 Env-based vaccine design. PubMed: 32385256DOI: 10.1038/s41467-020-16165-0 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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