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PDBsum entry 2lmp

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protein Protein-protein interface(s) links
Protein fibril PDB id
2lmp
Jmol
Contents
Protein chains
(+ 12 more) 32 a.a.
PDB id:
2lmp
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
Date:
08-Dec-11     Release date:   28-Dec-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05067  (A4_HUMAN) -  Amyloid beta A4 protein
Seq:
Struc:
 
Seq:
Struc:
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.
 
  ABSTRACT  
 
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
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.