5e61 | pdb_00005e61

Structure of amyloid-forming peptide FGAILSS (residues 23-29) from islet amyloid polypeptide

spinqualitylabelsall models 5e61, resolution 1.79Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5e61 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.79Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Structural studies of amyloidogenic segments by X-ray crystallography have revealed a novel packing motif, consisting of out-of-register beta sheets, that may constitute one of the toxic species in aggregation related diseases. Here we sought to determine the presence of such a motif in Islet amyloid polypeptide (IAPP), whose amyloidogenic properties are associated with Type 2 Diabetes. We determined four new crystal structures of segments within IAPP all forming steric zippers. Most interestingly, one of the segments in the fibril core of IAPP forms an out-of-register steric zipper. Analysis of this structure reveals several commonalities with previously solved out-of-register fibrils. Our results provide evidence that out-of-register beta sheets may be a common structural motif in amyloid aggregates and may be associated with toxicity. Crystal Structures of IAPP Amyloidogenic Segments Reveal a Novel Packing Motif of Out-of-Register Beta Sheets.,Soriaga AB, Sangwan S, Macdonald R, Sawaya MR, Eisenberg D J Phys Chem B. 2015 Dec 2. PMID:26629790 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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