6WXM
X-ray crystallographic structure of a beta-hairpin peptide derived from amyloid beta 16-36
Summary for 6WXM
| Entry DOI | 10.2210/pdb6wxm/pdb |
| Descriptor | Amyloid-beta protein, HEXANE-1,6-DIOL (3 entities in total) |
| Functional Keywords | oligomer, alzheimer's, de novo protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 11 |
| Total formula weight | 28536.03 |
| Authors | Kreutzer, A.G.,Nowick, J.S. (deposition date: 2020-05-11, release date: 2020-07-08, Last modification date: 2025-04-02) |
| Primary citation | Kreutzer, A.G.,Samdin, T.D.,Guaglianone, G.,Spencer, R.K.,Nowick, J.S. X-ray Crystallography Reveals Parallel and Antiparallel beta-Sheet Dimers of a beta-Hairpin Derived from A beta16-36that Assemble to Form Different Tetramers. Acs Chem Neurosci, 11:2340-2347, 2020 Cited by PubMed Abstract: High-resolution structures of oligomers formed by the β-amyloid peptide, Aβ, are important for understanding the molecular basis of Alzheimer's disease. Dimers of Aβ are linked to the pathogenesis and progression of Alzheimer's disease, and tetramers of Aβ 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 -terminal regions of Aβ. In the crystal lattice, the peptide assembles to form two different dimers-an antiparallel β-sheet dimer and a parallel β-sheet dimer-that each further self-assemble to form two different tetramers-a sandwich-like tetramer and a twisted β-sheet tetramer. The structures of these dimers and tetramers derived from Aβ serve as potential models for dimers and tetramers of full-length Aβ that form and in Alzheimer's disease-afflicted brains. PubMed: 32584538DOI: 10.1021/acschemneuro.0c00290 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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