6VLW
Crystal Structure of 426cOD in Complex with VRC01 Fab
Summary for 6VLW
| Entry DOI | 10.2210/pdb6vlw/pdb |
| Descriptor | VRC01 Fab Heavy Chain, VRC01 Fab Light Chain, 426cOD, ... (10 entities in total) |
| Functional Keywords | hiv, 426c, outer domain, vrc01, 426cod, fab, cd4, antibody, immunogen, immune system, immune system-viral protein complex, immune system/viral protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 3 |
| Total formula weight | 71511.99 |
| Authors | Weidle, C.,Pancera, M. (deposition date: 2020-01-27, release date: 2020-12-09, Last modification date: 2024-10-16) |
| Primary citation | Lin, Y.R.,Parks, K.R.,Weidle, C.,Naidu, A.S.,Khechaduri, A.,Riker, A.O.,Takushi, B.,Chun, J.H.,Borst, A.J.,Veesler, D.,Stuart, A.,Agrawal, P.,Gray, M.,Pancera, M.,Huang, P.S.,Stamatatos, L. HIV-1 VRC01 Germline-Targeting Immunogens Select Distinct Epitope-Specific B Cell Receptors. Immunity, 53:840-851.e6, 2020 Cited by PubMed Abstract: Activating precursor B cell receptors of HIV-1 broadly neutralizing antibodies requires specifically designed immunogens. Here, we compared the abilities of three such germline-targeting immunogens against the VRC01-class receptors to activate the targeted B cells in transgenic mice expressing the germline VH of the VRC01 antibody but diverse mouse light chains. Immunogen-specific VRC01-like B cells were isolated at different time points after immunization, their VH and VL genes were sequenced, and the corresponding antibodies characterized. VRC01 B cell sub-populations with distinct cross-reactivity properties were activated by each immunogen, and these differences correlated with distinct biophysical and biochemical features of the germline-targeting immunogens. Our study indicates that the design of effective immunogens to activate B cell receptors leading to protective HIV-1 antibodies will require a better understanding of how the biophysical properties of the epitope and its surrounding surface on the germline-targeting immunogen influence its interaction with the available receptor variants in vivo. PubMed: 33053332DOI: 10.1016/j.immuni.2020.09.007 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.42 Å) |
Structure validation
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