6wxm

X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36

spinqualitylabelsall models 6wxm, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: HEZ, ORN, PHI, SAR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed High-resolution structures of oligomers formed by the beta-amyloid peptide, Abeta, are important for understanding the molecular basis of Alzheimer's disease. Dimers of Abeta are linked to the pathogenesis and progression of Alzheimer's disease, and tetramers of Abeta are neurotoxic. This paper reports the X-ray crystallographic structures of dimers and tetramers, as well as an octamer, formed by a peptide derived from the central and C-terminal regions of Abeta. In the crystal lattice, the peptide assembles to form two different dimers-an antiparallel beta-sheet dimer and a parallel beta-sheet dimer-that each further self-assemble to form two different tetramers-a sandwich-like tetramer and a twisted beta-sheet tetramer. The structures of these dimers and tetramers derived from Abeta serve as potential models for dimers and tetramers of full-length Abeta that form in vitro and in Alzheimer's disease brains. X-Ray Crystallography Reveals Parallel and Antiparallel beta-Sheet Dimers of a beta-Hairpin Derived from Abeta16-36 that Assemble to Form Different Tetramers.,Kreutzer AG, Samdin TD, Guaglianone G, Spencer RK, Nowick JS ACS Chem Neurosci. 2020 Jun 25. doi: 10.1021/acschemneuro.0c00290. PMID:32584538 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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