7MDU
BG505 SOSIP MD39 in complex with the monoclonal antibodies Rh.33104 mAb.1 and RM20A3
Summary for 7MDU
| Entry DOI | 10.2210/pdb7mdu/pdb |
| EMDB information | 23778 23779 23780 |
| Descriptor | Rh.33104 mAb.1 Heavy Chain, Surface protein gp120, RM20A3 mAb Heavy Chain, ... (9 entities in total) |
| Functional Keywords | monoclonal antibody, immune complex, viral protein |
| Biological source | Macaca mulatta More |
| Total number of polymer chains | 6 |
| Total formula weight | 130957.74 |
| Authors | Antanasijevic, A.,Ward, A.B. (deposition date: 2021-04-06, release date: 2022-01-26, Last modification date: 2024-11-06) |
| Primary citation | Antanasijevic, A.,Bowman, C.A.,Kirchdoerfer, R.N.,Cottrell, C.A.,Ozorowski, G.,Upadhyay, A.A.,Cirelli, K.M.,Carnathan, D.G.,Enemuo, C.A.,Sewall, L.M.,Nogal, B.,Zhao, F.,Groschel, B.,Schief, W.R.,Sok, D.,Silvestri, G.,Crotty, S.,Bosinger, S.E.,Ward, A.B. From structure to sequence: Antibody discovery using cryoEM. Sci Adv, 8:eabk2039-eabk2039, 2022 Cited by PubMed Abstract: One of the rate-limiting steps in analyzing immune responses to vaccines or infections is the isolation and characterization of monoclonal antibodies. Here, we present a hybrid structural and bioinformatic approach to directly assign the heavy and light chains, identify complementarity-determining regions, and discover sequences from cryoEM density maps of serum-derived polyclonal antibodies bound to an antigen. When combined with next-generation sequencing of immune repertoires, we were able to specifically identify clonal family members, synthesize the monoclonal antibodies, and confirm that they interact with the antigen in a manner equivalent to the corresponding polyclonal antibodies. This structure-based approach for identification of monoclonal antibodies from polyclonal sera opens new avenues for analysis of immune responses and iterative vaccine design. PubMed: 35044813DOI: 10.1126/sciadv.abk2039 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
Download full validation report






