8OKR
virus enhancing amyloid fibril formed by CKFKFQF
Summary for 8OKR
| Entry DOI | 10.2210/pdb8okr/pdb |
| EMDB information | 16930 |
| Descriptor | PNF-18 (1 entity in total) |
| Functional Keywords | virus enhancing amyloid fibril, protein fibril, prion |
| Biological source | HIV whole-genome vector AA1305#18 |
| Total number of polymer chains | 24 |
| Total formula weight | 22780.03 |
| Authors | Heerde, T.,Schmidt, M.,Faendrich, M. (deposition date: 2023-03-29, release date: 2023-08-02, Last modification date: 2024-07-24) |
| Primary citation | Heerde, T.,Schutz, D.,Lin, Y.J.,Munch, J.,Schmidt, M.,Fandrich, M. Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril. Nat Commun, 14:4293-4293, 2023 Cited by PubMed Abstract: Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze the structure of a biotechnologically engineered peptide fibril that enhances retroviral infectivity. Our findings show that the peptide undergoes a time-dependent morphological maturation into polymorphic amyloid fibril structures. The fibrils consist of mated cross-β sheets that interact by the hydrophobic residues of the amphipathic fibril-forming peptide. The now available structural data help to explain the mechanism of retroviral infectivity enhancement, provide insights into the molecular plasticity of amyloid structures and illuminate the thermodynamic basis of their morphological maturation. PubMed: 37464004DOI: 10.1038/s41467-023-40042-1 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.86 Å) |
Structure validation
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