7WZ8
Structure of human langerin complex in Birbeck granules
This is a non-PDB format compatible entry.
Summary for 7WZ8
| Entry DOI | 10.2210/pdb7wz8/pdb |
| EMDB information | 32906 |
| Descriptor | SNAP-tag,C-type lectin domain family 4 member K (1 entity in total) |
| Functional Keywords | birbeck granule, c-type lectin, langerhans cell, virus defense, membrane protein |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 363286.64 |
| Authors | Oda, T.,Yanagisawa, H. (deposition date: 2022-02-17, release date: 2022-06-22, Last modification date: 2024-10-23) |
| Primary citation | Oda, T.,Yanagisawa, H.,Shinmori, H.,Ogawa, Y.,Kawamura, T. Cryo-electron tomography of Birbeck granules reveals the molecular mechanism of langerin lattice formation. Elife, 11:e79990-e79990, 2022 Cited by PubMed Abstract: Langerhans cells are specialized antigen-presenting cells localized within the epidermis and mucosal epithelium. Upon contact with Langerhans cells, pathogens are captured by the C-type lectin langerin and internalized into a structurally unique vesicle known as a Birbeck granule. Although the immunological role of Langerhans cells and Birbeck granules have been extensively studied, the mechanism by which the characteristic zippered membrane structure of Birbeck granules is formed remains elusive. In this study, we observed isolated Birbeck granules using cryo-electron tomography and reconstructed the 3D structure of the repeating unit of the honeycomb lattice of langerin at 6.4 Å resolution. We found that the interaction between the two langerin trimers was mediated by docking the flexible loop at residues 258-263 into the secondary carbohydrate-binding cleft. Mutations within the loop inhibited Birbeck granule formation and the internalization of HIV pseudovirus. These findings suggest a molecular mechanism for membrane zippering during Birbeck granule biogenesis and provide insight into the role of langerin in the defense against viral infection. PubMed: 35758632DOI: 10.7554/eLife.79990 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.4 Å) |
Structure validation
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