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PDBsum entry 2v17
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protein ligands Protein-protein interface(s) links
Immune system PDB id
2v17

 

 

 

 

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Contents
Protein chains
222 a.a. *
214 a.a. *
Ligands
THR-ASP-HIS-GLY-
ALA-GLU
Waters ×702
* Residue conservation analysis
PDB id:
2v17
Name: Immune system
Title: Structure of the complex of antibody mn423 with a fragment of tau protein
Structure: Peptide fragment. Chain: a. Monoclonal antibody fab fragment mn423. Chain: h. Other_details: disulphide bridge between l214 and h137 is reduced. Monoclonal antibody fab fragment mn423. Chain: l. Other_details: disulphide bridge between l214 and h137 is reduced
Source: Homo sapiens. Human. Organism_taxid: 9606. Cell_line: mn423 hybridoma. Organ: spleen. Cell: b-lymphocyte. Mus musculus. Mouse. Organism_taxid: 10090.
Resolution:
1.65Å     R-factor:   0.160     R-free:   0.218
Authors: J.Sevcik,R.Skrabana,N.Csokova,R.Dvorsky,M.Novak
Key ref: J.Sevcik et al. (2007). X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease. Febs Lett, 581, 5872-5878. PubMed id: 18061582
Date:
22-May-07     Release date:   25-Dec-07    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 222 a.a.
Protein chain
No UniProt id for this chain
Struc: 214 a.a.
Key:    Secondary structure  CATH domain

 

 
Febs Lett 581:5872-5878 (2007)
PubMed id: 18061582  
 
 
X-ray structure of the PHF core C-terminus: insight into the folding of the intrinsically disordered protein tau in Alzheimer's disease.
J.Sevcik, R.Skrabana, R.Dvorsky, N.Csokova, K.Iqbal, M.Novak.
 
  ABSTRACT  
 
The major constituent of Alzheimer's disease paired helical filaments (PHF) core is intrinsically disordered protein (IDP) tau. In spite of a considerable effort, insoluble character of PHF together with inherent physical properties of IDP tau have precluded so far reconstruction of PHF 3D structure by X-ray crystallography or NMR spectroscopy. Here we present first crystallographic study of PHF core C-terminus. Using monoclonal antibody MN423 specific to the tertiary structure of the PHF core, the in vivo PHF structure was imprinted into recombinant core PHF tau. Crystallization of the complex led to determination of the structure of the core PHF tau protein fragment 386TDHGAE391 at 1.65A resolution. Structural analysis suggests important role of the core PHF C-terminus for PHF assembly. It is reasonable to expect that this approach will help to reveal the structural principles underlying the tau protein assembly into PHF and possibly will facilitate rationale drug design for inhibition of Alzheimer neurofibrillary changes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19225878 B.Kovacech, N.Zilka, and M.Novak (2009).
New age of neuroproteomics in Alzheimer's disease research.
  Cell Mol Neurobiol, 29, 799-805.  
19893165 L.E.Rojo, J.Alzate-Morales, I.N.Saavedra, P.Davies, and R.B.Maccioni (2009).
Selective Interaction of Lansoprazole and Astemizole with Tau Polymers: Potential New Clinical Use in Diagnosis of Alzheimer's Disease.
  J Alzheimers Dis, (), 0.  
19226187 M.D.Mukrasch, S.Bibow, J.Korukottu, S.Jeganathan, J.Biernat, C.Griesinger, E.Mandelkow, and M.Zweckstetter (2009).
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution.
  PLoS Biol, 7, e34.  
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.

 

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