9hpp | pdb_00009hpp

Helical form of Citropin 1.3

spinqualitylabelsall models 9hpp, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9hpp is a 2 chain structure with sequence from Ranoidea citropa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.56Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CT13_RANCI Publication Abstract from PubMed Citropin 1.3 is an antimicrobial peptide secreted by the amphibian Litoria citropa (Southern bell frog). In this study, the structural and functional properties of its non-amidated form, which self-assembles into distinct fibrillar architectures, are investigated. Using cryogenic electron microscopy, X-ray crystallography, and fluorescence microscopy with model membranes and cells, diverse supramolecular structures, including canonical amyloid fibrils, multilayered nanotubes, and a novel mixed fibril type, are identified. In giant unilamellar vesicles, citropin 1.3 promoted membrane fusion and underwent lipid-induced phase separation. In mammalian cells, it permeabilized membranes, induced cell death, and colocalized with nucleic acids. These findings link antimicrobial activity to amyloid assembly and highlight the peptide's structural plasticity and potential biological functions, offering new insights into amyloid-based antimicrobial mechanisms. Structural and Functional Versatility of the Amyloidogenic Non-Amidated Variant of the Antimicrobial Peptide Citropin 1.3.,Strati F, Cali MP, Bloch Y, Mostafavi S, Monistrol J, Golubev A, Rayan B, Gustavsson E, Landau M Adv Sci (Weinh). 2025 Sep 28:e03997. doi: 10.1002/advs.202503997. PMID:41016026 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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