PDBsum entry 2lmp

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protein Protein-protein interface(s) links
Protein fibril PDB id
Protein chains
(+ 12 more) 32 a.a.
PDB id:
Name: Protein fibril
Title: Structural model for a 40-residue beta-amyloid fibril with t symmetry, positive stagger
Structure: Beta-amyloid protein 40. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r synonym: beta-app40. Engineered: yes
Source: Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 10 models
Authors: R.Tycko,A.Paravastu
Key ref: A.K.Paravastu et al. (2008). Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils. Proc Natl Acad Sci U S A, 105, 18349-18354. PubMed id: 19015532
08-Dec-11     Release date:   28-Dec-11    
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Protein chains
Pfam   ArchSchema ?
P05067  (A4_HUMAN) -  Amyloid beta A4 protein
770 a.a.
32 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   1 term 
  Biological process     nervous system development   1 term 


Proc Natl Acad Sci U S A 105:18349-18354 (2008)
PubMed id: 19015532  
Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils.
A.K.Paravastu, R.D.Leapman, W.M.Yau, R.Tycko.
We describe a full structural model for amyloid fibrils formed by the 40-residue beta-amyloid peptide associated with Alzheimer's disease (Abeta(1-40)), based on numerous constraints from solid state NMR and electron microscopy. This model applies specifically to fibrils with a periodically twisted morphology, with twist period equal to 120 +/- 20 nm (defined as the distance between apparent minima in fibril width in negatively stained transmission electron microscope images). The structure has threefold symmetry about the fibril growth axis, implied by mass-per-length data and the observation of a single set of (13)C NMR signals. Comparison with a previously reported model for Abeta(1-40) fibrils with a qualitatively different, striated ribbon morphology reveals the molecular basis for polymorphism. At the molecular level, the 2 Abeta(1-40) fibril morphologies differ in overall symmetry (twofold vs. threefold), the conformation of non-beta-strand segments, and certain quaternary contacts. Both morphologies contain in-register parallel beta-sheets, constructed from nearly the same beta-strand segments. Because twisted and striated ribbon morphologies are also observed for amyloid fibrils formed by other polypeptides, such as the amylin peptide associated with type 2 diabetes, these structural variations may have general implications.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21131979 C.Liu, M.R.Sawaya, and D.Eisenberg (2011).
β₂-microglobulin forms three-dimensional domain-swapped amyloid fibrils with disulfide linkages.
  Nat Struct Mol Biol, 18, 49-55.
PDB codes: 3low 3loz
22037310 N.L.Fawzi, J.Ying, R.Ghirlando, D.A.Torchia, and G.M.Clore (2011).
Atomic-resolution dynamics on the surface of amyloid-β protofibrils probed by solution NMR.
  Nature, 480, 268-272.  
19684598 J.J.Wiltzius, M.Landau, R.Nelson, M.R.Sawaya, M.I.Apostol, L.Goldschmidt, A.B.Soriaga, D.Cascio, K.Rajashankar, and D.Eisenberg (2009).
Molecular mechanisms for protein-encoded inheritance.
  Nat Struct Mol Biol, 16, 973-978.
PDB codes: 3fod 3fpo 3fqp 3fr1 3fth 3ftk 3ftl 3ftr 3fva
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