6P8M
Crystal Structure of Antibody P-p3b3 A60C Heavy Chain in Complex with 426c HIV-1 gp120 core G459C
Summary for 6P8M
| Entry DOI | 10.2210/pdb6p8m/pdb |
| Descriptor | Gp120, CHLORIDE ION, P-p3b3 Heavy Chain, ... (11 entities in total) |
| Functional Keywords | antibody, 426c, immunization, immune system |
| Biological source | Human immunodeficiency virus (HIV-1) More |
| Total number of polymer chains | 3 |
| Total formula weight | 91210.47 |
| Authors | Weidle, C.,Pancera, M. (deposition date: 2019-06-07, release date: 2019-11-20, Last modification date: 2024-11-06) |
| Primary citation | Parks, K.R.,MacCamy, A.J.,Trichka, J.,Gray, M.,Weidle, C.,Borst, A.J.,Khechaduri, A.,Takushi, B.,Agrawal, P.,Guenaga, J.,Wyatt, R.T.,Coler, R.,Seaman, M.,LaBranche, C.,Montefiori, D.C.,Veesler, D.,Pancera, M.,McGuire, A.,Stamatatos, L. Overcoming Steric Restrictions of VRC01 HIV-1 Neutralizing Antibodies through Immunization. Cell Rep, 29:3060-3072.e7, 2019 Cited by PubMed Abstract: Broadly HIV-1 neutralizing VRC01 class antibodies target the CD4-binding site of Env. They are derived from VH1-202 antibody heavy chains paired with rare light chains expressing 5-amino acid-long CDRL3s. They have been isolated from infected subjects but have not yet been elicited by immunization. Env-derived immunogens capable of binding the germline forms of VRC01 B cell receptors on naive B cells have been designed and evaluated in knockin mice. However, the elicited antibodies cannot bypass glycans present on the conserved position N276 of Env, which restricts access to the CD4-binding site. Efforts to guide the appropriate maturation of these antibodies by sequential immunization have not yet been successful. Here, we report on a two-step immunization scheme that leads to the maturation of VRC01-like antibodies capable of accommodating the N276 glycan and displaying autologous tier 2 neutralizing activities. Our results are relevant to clinical trials aiming to elicit VRC01 antibodies. PubMed: 31801073DOI: 10.1016/j.celrep.2019.10.071 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.594 Å) |
Structure validation
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