6W4M
CRYSTAL STRUCTURE OF THE ADCC-POTENT, WEAKLY NEUTRALIZING HIV ENV CO-RECEPTOR BINDING SITE ANTIBODY N12-I2 FAB IN COMPLEX WITH HIV-1 CLADE A/E GP120 AND M48U1
Replaces: 5UWESummary for 6W4M
| Entry DOI | 10.2210/pdb6w4m/pdb |
| Descriptor | clade A/E 93TH057 HIV-1 gp120 core, ANTI-HIV ANTIBODY N12-I2 FAB LIGHT CHAIN, ANTI-HIV ANTIBODY N12-I2 FAB HEAVY CHAIN, ... (5 entities in total) |
| Functional Keywords | adcc and neutralizing anti-hiv-1 env antibody n12-i2, cd4i antibody, fab fragment, hiv-1 gp120, immune system, clade a/e 93th057, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 4 |
| Total formula weight | 93456.73 |
| Authors | Tolbert, W.D.,Gohain, N.,Pazgier, M. (deposition date: 2020-03-11, release date: 2020-08-05, Last modification date: 2023-11-15) |
| Primary citation | Tolbert, W.D.,Sherburn, R.,Gohain, N.,Ding, S.,Flinko, R.,Orlandi, C.,Ray, K.,Finzi, A.,Lewis, G.K.,Pazgier, M. Defining rules governing recognition and Fc-mediated effector functions to the HIV-1 co-receptor binding site. Bmc Biol., 18:91-91, 2020 Cited by PubMed Abstract: The binding of HIV-1 Envelope glycoproteins (Env) to host receptor CD4 exposes vulnerable conserved epitopes within the co-receptor binding site (CoRBS) which are required for the engagement of either CCR5 or CXCR4 co-receptor to allow HIV-1 entry. Antibodies against this region have been implicated in the protection against HIV acquisition in non-human primate (NHP) challenge studies and found to act synergistically with antibodies of other specificities to deliver effective Fc-mediated effector function against HIV-1-infected cells. Here, we describe the structure and function of N12-i2, an antibody isolated from an HIV-1-infected individual, and show how the unique structural features of this antibody allow for its effective Env recognition and Fc-mediated effector function. PubMed: 32693837DOI: 10.1186/s12915-020-00819-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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