5VJO
Complex between HyHEL10 Fab fragment heavy chain mutant I29F and Pekin duck egg lysozyme isoform I (DEL-I)
Summary for 5VJO
| Entry DOI | 10.2210/pdb5vjo/pdb |
| Related | 5VJQ |
| Descriptor | HyHEL10 heavy chain Fab fragment carrying I29F mutation., HyHEL10 light chain Fab fragment, lysozyme isoform I (DEL-I), ... (6 entities in total) |
| Functional Keywords | lysozyme, hydrolase, hydrolase-immune system complex, hydrolase/immune system |
| Biological source | Mus musculus More |
| Total number of polymer chains | 6 |
| Total formula weight | 121777.72 |
| Authors | Langley, D.B.,Christ, D. (deposition date: 2017-04-19, release date: 2018-04-11, Last modification date: 2024-10-09) |
| Primary citation | Burnett, D.L.,Langley, D.B.,Schofield, P.,Hermes, J.R.,Chan, T.D.,Jackson, J.,Bourne, K.,Reed, J.H.,Patterson, K.,Porebski, B.T.,Brink, R.,Christ, D.,Goodnow, C.C. Germinal center antibody mutation trajectories are determined by rapid self/foreign discrimination. Science, 360:223-226, 2018 Cited by PubMed Abstract: Antibodies have the specificity to differentiate foreign antigens that mimic self antigens, but it remains unclear how such specificity is acquired. In a mouse model, we generated B cells displaying an antibody that cross-reacts with two related protein antigens expressed on self versus foreign cells. B cell anergy was imposed by self antigen but reversed upon challenge with high-density foreign antigen, leading to germinal center recruitment and antibody gene hypermutation. Single-cell analysis detected rapid selection for mutations that decrease self affinity and slower selection for epistatic mutations that specifically increase foreign affinity. Crystal structures revealed that these mutations exploited subtle topological differences to achieve 5000-fold preferential binding to foreign over self epitopes. Resolution of antigenic mimicry drove the optimal affinity maturation trajectory, highlighting the value of retaining self-reactive clones as substrates for protective antibody responses. PubMed: 29650674DOI: 10.1126/science.aao3859 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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