2MVX

Atomic-resolution 3D structure of amyloid-beta fibrils: the Osaka mutation


Experimental Data Snapshot

  • Method: SOLID-STATE NMR
  • Conformers Calculated: 500 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

Atomic-Resolution Three-Dimensional Structure of Amyloid beta Fibrils Bearing the Osaka Mutation.

Schutz, A.K.Vagt, T.Huber, M.Ovchinnikova, O.Y.Cadalbert, R.Wall, J.Guntert, P.Bockmann, A.Glockshuber, R.Meier, B.H.

(2015) Angew Chem Int Ed Engl 54: 331-335

  • DOI: https://doi.org/10.1002/anie.201408598
  • Primary Citation of Related Structures:  
    2MVX

  • PubMed Abstract: 

    Despite its central importance for understanding the molecular basis of Alzheimer's disease (AD), high-resolution structural information on amyloid β-peptide (Aβ) fibrils, which are intimately linked with AD, is scarce. We report an atomic-resolution fibril structure of the Aβ1-40 peptide with the Osaka mutation (E22Δ), associated with early-onset AD. The structure, which differs substantially from all previously proposed models, is based on a large number of unambiguous intra- and intermolecular solid-state NMR distance restraints.


  • Organizational Affiliation

    Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093 Zurich (Switzerland).


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, J
39Homo sapiensMutation(s): 0 
Gene Names: A4AD1APP
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: 500 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2014-11-26
    Type: Initial release
  • Version 1.1: 2015-01-21
    Changes: Database references