5CCK
Crystal structure of Human anti-HIV-1 broadly neutralizing antibody 3BC315 Fab
Summary for 5CCK
| Entry DOI | 10.2210/pdb5cck/pdb |
| Related | 5AWN |
| EMDB information | 3067 |
| Descriptor | Antibody 3BC315 Fab heavy chain, Antibody 3BC315 Fab light chain, 3-CYCLOHEXYL-1-PROPYLSULFONIC ACID, ... (4 entities in total) |
| Functional Keywords | hiv-1, env, bnab, antibody, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 2 |
| Total formula weight | 48230.16 |
| Authors | Lee, J.H.,Ward, A.B.,Wilson, I.A. (deposition date: 2015-07-02, release date: 2015-10-07, Last modification date: 2024-10-16) |
| Primary citation | Lee, J.H.,Leaman, D.P.,Kim, A.S.,Torrents de la Pena, A.,Sliepen, K.,Yasmeen, A.,Derking, R.,Ramos, A.,de Taeye, S.W.,Ozorowski, G.,Klein, F.,Burton, D.R.,Nussenzweig, M.C.,Poignard, P.,Moore, J.P.,Klasse, P.J.,Sanders, R.W.,Zwick, M.B.,Wilson, I.A.,Ward, A.B. Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike. Nat Commun, 6:8167-8167, 2015 Cited by PubMed Abstract: The recent identification of three broadly neutralizing antibodies (bnAbs) against gp120-gp41 interface epitopes has expanded the targetable surface on the HIV-1 envelope glycoprotein (Env) trimer. By using biochemical, biophysical and computational methods, we map the previously unknown trimer epitopes of two related antibodies, 3BC315 and 3BC176. A cryo-EM reconstruction of a soluble Env trimer bound to 3BC315 Fab at 9.3 Å resolution reveals that the antibody binds between two gp41 protomers, and neutralizes the virus by accelerating trimer decay. In contrast, bnAb 35O22 binding to a partially overlapping quaternary epitope at the gp120-gp41 interface does not induce decay. A conserved gp41-proximal glycan at N88 was also shown to play a role in the binding kinetics of 3BC176 and 3BC315. Finally, our data suggest that the dynamic structure of the Env trimer influences exposure of bnAb epitopes. PubMed: 26404402DOI: 10.1038/ncomms9167 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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