8okr

virus enhancing amyloid fibril formed by CKFKFQF

spinqualitylabelsall models 8okr, resolution 2.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8okr is a 24 chain structure with sequence from HIV whole-genome vector AA1305#18. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.86Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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-beta 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. Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril.,Heerde T, Schutz D, Lin YJ, Munch J, Schmidt M, Fandrich M Nat Commun. 2023 Jul 18;14(1):4293. doi: 10.1038/s41467-023-40042-1. PMID:37464004 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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