3Q9H
LVFFA segment from Alzheimer's Amyloid-Beta displayed on 42-membered macrocycle scaffold
Summary for 3Q9H
| Entry DOI | 10.2210/pdb3q9h/pdb |
| Related | 3Q9G 3Q9I 3Q9J |
| Descriptor | Cyclic pseudo-peptide LVFFA(ORN)(HAO)LK(ORN), SULFATE ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | beta sheet tetramer, macrocyclic peptide, beta-sheet mimetic, protein fibril |
| Total number of polymer chains | 8 |
| Total formula weight | 12440.61 |
| Authors | Liu, C.,Sawaya, M.R.,Eisenberg, D.,Nowick, J.S.,Cheng, P.,Zheng, J. (deposition date: 2011-01-07, release date: 2011-06-08, Last modification date: 2023-11-15) |
| Primary citation | Liu, C.,Sawaya, M.R.,Cheng, P.N.,Zheng, J.,Nowick, J.S.,Eisenberg, D. Characteristics of Amyloid-Related Oligomers Revealed by Crystal Structures of Macrocyclic beta-Sheet Mimics. J.Am.Chem.Soc., 133:6736-6744, 2011 Cited by PubMed Abstract: Protein amyloid oligomers have been strongly linked to amyloid diseases and can be intermediates to amyloid fibers. β-Sheets have been identified in amyloid oligomers. However, because of their transient and highly polymorphic properties, the details of their self-association remain elusive. Here we explore oligomer structure using a model system: macrocyclic peptides. Key amyloidogenic sequences from Aβ and tau were incorporated into macrocycles, thereby restraining them to β-strands, but limiting the growth of the oligomers so they may crystallize and cannot fibrillate. We determined the atomic structures for four such oligomers, and all four reveal tetrameric interfaces in which β-sheet dimers pair together by highly complementary, dry interfaces, analogous to steric zippers found in fibers, suggesting a common structure for amyloid oligomers and fibers. In amyloid fibers, the axes of the paired sheets are either parallel or antiparallel, whereas the oligomeric interfaces display a variety of sheet-to-sheet pairing angles, offering a structural explanation for the heterogeneity of amyloid oligomers. PubMed: 21473620DOI: 10.1021/ja200222n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.25 Å) |
Structure validation
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