6OPA
Crystal structure of bovine Fab NC-Cow1 in complex with HIV-1 BG505 SOSIP.664, and human Fabs 35022 and PGT128
Summary for 6OPA
| Entry DOI | 10.2210/pdb6opa/pdb |
| Descriptor | Envelope glycoprotein gp160, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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 | hiv-1 broadly neutralizing antibody, viral protein-immune system complex, immune system |
| Biological source | Human immunodeficiency virus 1 More |
| Total number of polymer chains | 8 |
| Total formula weight | 229340.44 |
| Authors | Stanfield, R.L.,Wilson, I.A. (deposition date: 2019-04-24, release date: 2020-04-01, Last modification date: 2024-11-13) |
| Primary citation | Stanfield, R.L.,Berndsen, Z.T.,Huang, R.,Sok, D.,Warner, G.,Torres, J.L.,Burton, D.R.,Ward, A.B.,Wilson, I.A.,Smider, V.V. Structural basis of broad HIV neutralization by a vaccine-induced cow antibody. Sci Adv, 6:eaba0468-eaba0468, 2020 Cited by PubMed Abstract: Potent broadly neutralizing antibodies (bnAbs) to HIV have been very challenging to elicit by vaccination in wild-type animals. Here, by x-ray crystallography, cryo-electron microscopy, and site-directed mutagenesis, we structurally and functionally elucidate the mode of binding of a potent bnAb (NC-Cow1) elicited in cows by immunization with the HIV envelope (Env) trimer BG505 SOSIP.664. The exceptionally long (60 residues) third complementarity-determining region of the heavy chain (CDR H3) of NC-Cow1 forms a mini domain (knob) on an extended stalk that navigates through the dense glycan shield on Env to target a small footprint on the gp120 CD4 receptor binding site with no contact of the other CDRs to the rest of the Env trimer. These findings illustrate, in molecular detail, how an unusual vaccine-induced cow bnAb to HIV Env can neutralize with high potency and breadth. PubMed: 32518821DOI: 10.1126/sciadv.aba0468 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (4.084 Å) |
Structure validation
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