6URH
Crystal structure of broadly neutralizing antibody AR3X in complex with Hepatitis C virus envelope glycoprotein E2 ectodomain
Summary for 6URH
| Entry DOI | 10.2210/pdb6urh/pdb |
| Descriptor | HCV envelope glycoprotein E2, AR3X Heavy Chain, AR3X Light Chain, ... (9 entities in total) |
| Functional Keywords | hcv glycoprotein, broadly neutralizing antibodies, viral protein-immune system complex, viral protein/immune system |
| Biological source | Hepacivirus C More |
| Total number of polymer chains | 3 |
| Total formula weight | 83121.19 |
| Authors | Flyak, A.I.,Bjorkman, P.J. (deposition date: 2019-10-23, release date: 2020-03-18, Last modification date: 2024-10-30) |
| Primary citation | Flyak, A.I.,Ruiz, S.E.,Salas, J.,Rho, S.,Bailey, J.R.,Bjorkman, P.J. An ultralong CDRH2 in HCV neutralizing antibody demonstrates structural plasticity of antibodies against E2 glycoprotein. Elife, 9:-, 2020 Cited by PubMed Abstract: A vaccine protective against diverse HCV variants is needed to control the HCV epidemic. Structures of E2 complexes with front layer-specific broadly neutralizing antibodies (bNAbs) isolated from HCV-infected individuals, revealed a disulfide bond-containing CDRH3 that adopts straight (individuals who clear infection) or bent (individuals with chronic infection) conformation. To investigate whether a straight versus bent disulfide bond-containing CDRH3 is specific to particular HCV-infected individuals, we solved a crystal structure of the HCV E2 ectodomain in complex with AR3X, a bNAb with an unusually long CDRH2 that was isolated from the chronically-infected individual from whom the bent CDRH3 bNAbs were derived. The structure revealed that AR3X utilizes both its ultralong CDRH2 and a disulfide motif-containing straight CDRH3 to recognize the E2 front layer. These results demonstrate that both the straight and bent CDRH3 classes of HCV bNAb can be elicited in a single individual, revealing a structural plasticity of -derived bNAbs. PubMed: 32125272DOI: 10.7554/eLife.53169 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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