2M9S
3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside
Summary for 2M9S
| Entry DOI | 10.2210/pdb2m9s/pdb |
| Related | 2M9R |
| Descriptor | Amyloid beta A4 protein, (2S,3S)-3-(3,5-dihydroxyphenyl)-2-(4-hydroxyphenyl)-4-[(E)-2-(4-hydroxyphenyl)ethenyl]-2,3-dihydro-1-benzofuran-6-yl beta-D-glucopyranoside (2 entities in total) |
| Functional Keywords | amyloid peptide, protein fibril |
| Biological source | Homo sapiens (human) |
| Cellular location | Membrane; Single-pass type I membrane protein: P05067 |
| Total number of polymer chains | 1 |
| Total formula weight | 5569.07 |
| Authors | Monti, J.,Richard, T. (deposition date: 2013-06-19, release date: 2013-09-11, Last modification date: 2024-05-01) |
| Primary citation | Richard, T.,Papastamoulis, Y.,Pierre, W.T.,Monti, J.P. 3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside: Implications in Alzheimer's disease. Biochim.Biophys.Acta, 1830:5068-5074, 2013 Cited by PubMed Abstract: Alzheimer's disease (AD) is a progressive neurodegenerative disorder. There is a consensus that Aβ is a pathologic agent and that its toxic effects, which are at present incompletely understood, may occur through several potential mechanisms. Polyphenols are known to have wide-ranging properties with regard to health and for helping to prevent various diseases like neurodegenerative disorders. Thus inhibiting the formation of toxic Aβ assemblies is a reasonable hypothesis to prevent and perhaps treat AD METHODS: Solution NMR and molecular modeling were used to obtain more information about the interaction between the Aβ1-40 and the polyphenol ε-viniferin glucoside (EVG) and particularly the Aβ residues involved in the complex. PubMed: 23830862DOI: 10.1016/j.bbagen.2013.06.031 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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