9JKF
Asymmetric structure of cleaved HIV-1 Tri FPPR envelope glycoprotein trimer in amphipol-lipid nanodiscs (Tri FPPR.1)
This is a non-PDB format compatible entry.
Summary for 9JKF
| Entry DOI | 10.2210/pdb9jkf/pdb |
| EMDB information | 61553 |
| Descriptor | Envelope glycoprotein gp160, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (15 entities in total) |
| Functional Keywords | viral entry, viral protein |
| Biological source | Simian-Human immunodeficiency virus |
| Total number of polymer chains | 6 |
| Total formula weight | 540616.52 |
| Authors | Qi, Y.,Zhang, S.,Sodroski, J.,Mao, Y. (deposition date: 2024-09-16, release date: 2025-02-26, Last modification date: 2025-04-02) |
| Primary citation | Qi, Y.,Zhang, S.,Wang, K.,Ding, H.,Zhang, Z.,Anang, S.,Nguyen, H.T.,Kappes, J.C.,Sodroski, J.,Mao, Y. The membrane-proximal external region of human immunodeficiency virus (HIV-1) envelope glycoprotein trimers in A18-lipid nanodiscs. Commun Biol, 8:442-442, 2025 Cited by PubMed Abstract: During human immunodeficiency virus (HIV-1) entry, the metastable pretriggered envelope glycoprotein (Env) trimer ((gp120/gp41)) opens asymmetrically. We present cryo-EM structures of cleaved asymmetric Env trimers in amphipol-lipid nanodiscs. The gp41 membrane-proximal external region (MPER) could be traced in Env protomers that remained close to the nanodisc despite Env tilting. The MPER interacts with the gp120 C-termini and gp41 α9 helices at the base of the Env trimer. MPER conformation is coupled with the tilt angles of the α9 helices, the helicity of the gp41 heptad repeat (HR1) regions, and the opening angles between the protomers of the asymmetric trimers. Our structural models explain the stabilizing effects of MPER integrity and Env proteolytic maturation on the pretriggered Env conformation. Superimposed on the asymmetry of the Env protomers, variation in the glycans at the trimer apex creates substantial structural heterogeneity in the V2 quaternary epitopes of difficult-to-elicit broadly neutralizing antibodies. PubMed: 40089599DOI: 10.1038/s42003-025-07852-z PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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