3RPI
Crystal Structure of Fab from 3BNC60, Highly Potent anti-HIV Antibody
Summary for 3RPI
| Entry DOI | 10.2210/pdb3rpi/pdb |
| Descriptor | Light chain from highly potent anti-HIV neutralizing antibody, Heavy chain from highly potent anti-HIV neutralizing antibody, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | igg, glycosylation, immune system |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 4 |
| Total formula weight | 96411.41 |
| Authors | Diskin, R.,Bjorkman, P.J. (deposition date: 2011-04-26, release date: 2011-07-20, Last modification date: 2024-11-27) |
| Primary citation | Scheid, J.F.,Mouquet, H.,Ueberheide, B.,Diskin, R.,Klein, F.,Oliveira, T.Y.,Pietzsch, J.,Fenyo, D.,Abadir, A.,Velinzon, K.,Hurley, A.,Myung, S.,Boulad, F.,Poignard, P.,Burton, D.R.,Pereyra, F.,Ho, D.D.,Walker, B.D.,Seaman, M.S.,Bjorkman, P.J.,Chait, B.T.,Nussenzweig, M.C. Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding. Science, 333:1633-1637, 2011 Cited by PubMed Abstract: Passive transfer of broadly neutralizing HIV antibodies can prevent infection, which suggests that vaccines that elicit such antibodies would be protective. Thus far, however, few broadly neutralizing HIV antibodies that occur naturally have been characterized. To determine whether these antibodies are part of a larger group of related molecules, we cloned 576 new HIV antibodies from four unrelated individuals. All four individuals produced expanded clones of potent broadly neutralizing CD4-binding-site antibodies that mimic binding to CD4. Despite extensive hypermutation, the new antibodies shared a consensus sequence of 68 immunoglobulin H (IgH) chain amino acids and arise independently from two related IgH genes. Comparison of the crystal structure of one of the antibodies to the broadly neutralizing antibody VRC01 revealed conservation of the contacts to the HIV spike. PubMed: 21764753DOI: 10.1126/science.1207227 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.648 Å) |
Structure validation
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