2PV6
HIV-1 gp41 Membrane Proximal Ectodomain Region peptide in DPC micelle
Summary for 2PV6
| Entry DOI | 10.2210/pdb2pv6/pdb |
| Descriptor | Envelope glycoprotein (1 entity in total) |
| Functional Keywords | kinked helix, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Cellular location | Transmembrane protein gp41: Virion membrane; Single-pass type I membrane protein. Surface protein gp120: Virion membrane; Peripheral membrane protein: P04578 |
| Total number of polymer chains | 1 |
| Total formula weight | 2929.33 |
| Authors | Sun, Z.-Y.J.,Oh, K.J.,Kim, M.,Reinherz, E.L.,Wagner, G. (deposition date: 2007-05-09, release date: 2008-03-18, Last modification date: 2024-05-22) |
| Primary citation | Sun, Z.Y.,Oh, K.J.,Kim, M.,Yu, J.,Brusic, V.,Song, L.,Qiao, Z.,Wang, J.H.,Wagner, G.,Reinherz, E.L. HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane Immunity, 28:52-63, 2008 Cited by PubMed Abstract: Although rarely elicited during natural human infection, the most broadly neutralizing antibodies (BNAbs) against diverse human immunodeficiency virus (HIV)-1 strains target the membrane-proximal ectodomain region (MPER) of viral gp41. To gain insight into MPER antigenicity, immunogenicity, and viral function, we studied its structure in the lipid environment by a combination of nuclear magnetic resonance (NMR), electron paramagnetic resonance (EPR), and surface plasmon resonance (SPR) techniques. The analyses revealed a tilted N-terminal alpha helix (aa 664-672) connected via a short hinge to a flat C-terminal helical segment (675-683). This metastable L-shaped structure is immersed in viral membrane and, therefore, less accessible to immune attack. Nonetheless, the 4E10 BNAb extracts buried W672 and F673 after initial encounter with the surface-embedded MPER. The data suggest how BNAbs may perturb tryptophan residue-associated viral fusion involving the mobile N-terminal MPER segment and, given conservation of MPER sequences in HIV-1, HIV-2, and SIV, have important implications for structure-guided vaccine design. PubMed: 18191596DOI: 10.1016/j.immuni.2007.11.018 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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