2M4J

40-residue beta-amyloid fibril derived from Alzheimer's disease brain


Experimental Data Snapshot

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 600 
  • Conformers Submitted: 20 
  • Selection Criteria: no violations, low restraint energy, and maximum structural diversity 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Molecular Structure of beta-Amyloid Fibrils in Alzheimer's Disease Brain Tissue.

Lu, J.X.Qiang, W.Yau, W.M.Schwieters, C.D.Meredith, S.C.Tycko, R.

(2013) Cell 154: 1257-1268

  • DOI: https://doi.org/10.1016/j.cell.2013.08.035
  • Primary Citation of Related Structures:  
    2M4J

  • PubMed Abstract: 

    In vitro, β-amyloid (Aβ) peptides form polymorphic fibrils, with molecular structures that depend on growth conditions, plus various oligomeric and protofibrillar aggregates. Here, we investigate structures of human brain-derived Aβ fibrils, using seeded fibril growth from brain extract and data from solid-state nuclear magnetic resonance and electron microscopy. Experiments on tissue from two Alzheimer's disease (AD) patients with distinct clinical histories showed a single predominant 40 residue Aβ (Aβ40) fibril structure in each patient; however, the structures were different from one another. A molecular structural model developed for Aβ40 fibrils from one patient reveals features that distinguish in-vivo- from in-vitro-produced fibrils. The data suggest that fibrils in the brain may spread from a single nucleation site, that structural variations may correlate with variations in AD, and that structure-specific amyloid imaging agents may be an important future goal.


  • Organizational Affiliation

    Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Amyloid beta A4 protein
A, B, C, D, E
A, B, C, D, E, F, G, H, I
40Homo sapiensMutation(s): 0 
UniProt & NIH Common Fund Data Resources
Find proteins for P05067 (Homo sapiens)
Explore P05067 
Go to UniProtKB:  P05067
PHAROS:  P05067
GTEx:  ENSG00000142192 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP05067
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 600 
  • Conformers Submitted: 20 
  • Selection Criteria: no violations, low restraint energy, and maximum structural diversity 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-09-25
    Type: Initial release
  • Version 1.1: 2013-10-02
    Changes: Database references
  • Version 1.2: 2023-06-14
    Changes: Data collection, Database references, Other