8onq

Structure of the amyloid-forming peptide Ac-EFIAWL from human GLP-1

spinqualitylabelsall models 8onq, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8onq is a 2 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.5Å Ligands: ACE Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed A large group of hormones are stored as amyloid fibrils in acidic secretion vesicles before they are released into the bloodstream and readopt their functional state. Here, we identify an evolutionarily conserved hexapeptide sequence as the major aggregation-prone region (APR) of gastrointestinal peptides of the glucagon family: xFxxWL. We determine nine polymorphic crystal structures of the APR segments of glucagon-like peptides 1 and 2, and exendin and its derivatives. We follow amyloid formation by CD, FTIR, ThT assays, and AFM. We propose that the pH-dependent changes of the protonation states of glutamate/aspartate residues of APRs initiate switching between the amyloid and the folded, monomeric forms of the hormones. We find that pH sensitivity diminishes in the absence of acidic gatekeepers and amyloid formation progresses over a broad pH range. Our results highlight the dual role of short aggregation core motifs in reversible amyloid formation and receptor binding. Polymorphic amyloid nanostructures of hormone peptides involved in glucose homeostasis display reversible amyloid formation.,Horvath D, Durvanger Z, K Menyhard D, Sulyok-Eiler M, Bencs F, Gyulai G, Horvath P, Taricska N, Perczel A Nat Commun. 2023 Aug 1;14(1):4621. doi: 10.1038/s41467-023-40294-x. PMID:37528104 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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