6OC7
HMP42 Fab in complex with Protein G
Summary for 6OC7
| Entry DOI | 10.2210/pdb6oc7/pdb |
| Descriptor | Heavy chain of HMP42 Fab, Light chain for HMP42 Fab, Immunoglobulin G-binding protein G, ... (4 entities in total) |
| Functional Keywords | anti-hiv antibody, fab fragment, crystallization chaperone, immune system |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 3 |
| Total formula weight | 55318.46 |
| Authors | Bernard, S.M.,Wilson, I.A. (deposition date: 2019-03-22, release date: 2020-02-05, Last modification date: 2024-10-23) |
| Primary citation | Steichen, J.M.,Lin, Y.C.,Havenar-Daughton, C.,Pecetta, S.,Ozorowski, G.,Willis, J.R.,Toy, L.,Sok, D.,Liguori, A.,Kratochvil, S.,Torres, J.L.,Kalyuzhniy, O.,Melzi, E.,Kulp, D.W.,Raemisch, S.,Hu, X.,Bernard, S.M.,Georgeson, E.,Phelps, N.,Adachi, Y.,Kubitz, M.,Landais, E.,Umotoy, J.,Robinson, A.,Briney, B.,Wilson, I.A.,Burton, D.R.,Ward, A.B.,Crotty, S.,Batista, F.D.,Schief, W.R. A generalized HIV vaccine design strategy for priming of broadly neutralizing antibody responses. Science, 366:-, 2019 Cited by PubMed Abstract: Vaccine induction of broadly neutralizing antibodies (bnAbs) to HIV remains a major challenge. Germline-targeting immunogens hold promise for initiating the induction of certain bnAb classes; yet for most bnAbs, a strong dependence on antibody heavy chain complementarity-determining region 3 (HCDR3) is a major barrier. Exploiting ultradeep human antibody sequencing data, we identified a diverse set of potential antibody precursors for a bnAb with dominant HCDR3 contacts. We then developed HIV envelope trimer-based immunogens that primed responses from rare bnAb-precursor B cells in a mouse model and bound a range of potential bnAb-precursor human naïve B cells in ex vivo screens. Our repertoire-guided germline-targeting approach provides a framework for priming the induction of many HIV bnAbs and could be applied to most HCDR3-dominant antibodies from other pathogens. PubMed: 31672916DOI: 10.1126/science.aax4380 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.296 Å) |
Structure validation
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