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PDBsum entry 4hix

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protein ligands Protein-protein interface(s) links
Protein fibril/immune system PDB id
4hix
Jmol
Contents
Protein chains
219 a.a.
219 a.a.
Ligands
ASP-ALA-GLU-PHE-
ARG-HIS
Waters ×237
PDB id:
4hix
Name: Protein fibril/immune system
Title: Crystal structure of a humanised 3d6 fab bound to amyloid be
Structure: Humanized 3d6 fab heavy chain. Chain: h. Engineered: yes. Humanized 3d6 fab light chain. Chain: l. Engineered: yes. Beta-amyloid protein 40. Chain: a. Synonym: beta-app40.
Source: Homo sapiens, mus musculus. Human, mouse. Organism_taxid: 9606, 10090. Synthetic: yes. Homo sapiens. Human. Organism_taxid: 9606
Resolution:
2.20Å     R-factor:   0.174     R-free:   0.220
Authors: L.A.Miles,G.A.N.Crespi,M.W.Parker
Key ref: L.A.Miles et al. (2013). Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation. Sci Rep, 3, 1302. PubMed id: 23416764
Date:
12-Oct-12     Release date:   13-Mar-13    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 219 a.a.
Protein chain
Pfam   ArchSchema ?
P01834  (IGKC_HUMAN) -  Ig kappa chain C region
Seq:
Struc:
106 a.a.
219 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   5 terms 
  Biological process     Fc-epsilon receptor signaling pathway   8 terms 
  Biochemical function     antigen binding     1 term  

 

 
Sci Rep 3:1302 (2013)
PubMed id: 23416764  
 
 
Bapineuzumab captures the N-terminus of the Alzheimer's disease amyloid-beta peptide in a helical conformation.
L.A.Miles, G.A.Crespi, L.Doughty, M.W.Parker.
 
  ABSTRACT  
 
Bapineuzumab is a humanized antibody developed by Pfizer and Johnson & Johnson targeting the amyloid (Aβ) plaques that underlie Alzheimer's disease neuropathology. Here we report the crystal structure of a Fab-Aβ peptide complex that reveals Bapineuzumab surprisingly captures Aβ in a monomeric helical conformation at the N-terminus. Microscale thermophoresis suggests that the Fab binds soluble Aβ(1-40) with a K(D) of 89 (±9) nM. The structure explains the antibody's exquisite selectivity for particular Aβ species and why it cannot recognize N-terminally modified or truncated Aβ peptides.