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PDBsum entry 1bjc

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protein links
Glycoprotein PDB id
1bjc
Jmol
Contents
Protein chain
28 a.a.
PDB id:
1bjc
Name: Glycoprotein
Title: Solution nmr structure of amyloid beta[f16], residues 1-28, 15 structures
Structure: Amyloid beta-peptide. Chain: a. Fragment: abeta [f16], residues 1-28. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: unidentified. Expression_system_taxid: 32644
NMR struc: 15 models
Authors: S.-A.Poulsen,A.A.Watson,D.J.Craik
Key ref: S.A.Poulsen et al. (2000). Solution structures in aqueous SDS micelles of two amyloid beta peptides of A beta(1-28) mutated at the alpha-secretase cleavage site (K16E, K16F). J Struct Biol, 130, 142-152. PubMed id: 10940222 DOI: 10.1006/jsbi.2000.4267
Date:
23-Jun-98     Release date:   18-Nov-98    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P05067  (A4_HUMAN) -  Amyloid beta A4 protein
Seq:
Struc:
 
Seq:
Struc:
770 a.a.
28 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     integral to membrane   1 term 

 

 
DOI no: 10.1006/jsbi.2000.4267 J Struct Biol 130:142-152 (2000)
PubMed id: 10940222  
 
 
Solution structures in aqueous SDS micelles of two amyloid beta peptides of A beta(1-28) mutated at the alpha-secretase cleavage site (K16E, K16F).
S.A.Poulsen, A.A.Watson, D.P.Fairlie, D.J.Craik.
 
  ABSTRACT  
 
NMRsolution structures are reported for two mutants (K16E, K16F) of the soluble amyloid beta peptide Abeta(1-28). The structural effects of these mutations of a positively charged residue to anionic and hydrophobic residues at the alpha-secretase cleavage site (Lys16-Leu17) were examined in the membrane-simulating solvent aqueous SDS micelles. Overall the three-dimensional structures were similar to that for the native Abeta(1-28) sequence in that they contained an unstructured N-terminus and a helical C-terminus. These structural elements are similar to those seen in the corresponding regions of full-length Abeta peptides Abeta(1-40) and Abeta(1-42), showing that the shorter peptides are valid model systems. The K16E mutation, which might be expected to stabilize the macrodipole of the helix, slightly increased the helix length (residues 13-24) relative to the K16F mutation, which shortened the helix to between residues 16 and 24. The observed sequence-dependent control over conformation in this region provides an insight into possible conformational switching roles of mutations in the amyloid precursor protein from which Abeta peptides are derived. In addition, if conformational transitions from helix to random coil to sheet precede aggregation of Abeta peptides in vivo, as they do in vitro, the conformation-inducing effects of mutations at Lys16 may also influence aggregation and fibril formation.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18702528 A.J.Beel, C.K.Mobley, H.J.Kim, F.Tian, A.Hadziselimovic, B.Jap, J.H.Prestegard, and C.R.Sanders (2008).
Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP): does APP function as a cholesterol sensor?
  Biochemistry, 47, 9428-9446.  
18399201 E.Gaggelli, Z.Grzonka, H.Kozłowski, C.Migliorini, E.Molteni, D.Valensin, and G.Valensin (2008).
Structural features of the Cu(II) complex with the rat Abeta(1-28) fragment.
  Chem Commun (Camb), (), 341-343.  
  18453721 K.S.Wun, L.A.Miles, G.A.Crespi, K.Wycherley, D.B.Ascher, K.J.Barnham, R.Cappai, K.Beyreuther, C.L.Masters, M.W.Parker, and W.J.McKinstry (2008).
Crystallization and preliminary X-ray diffraction analysis of the Fab fragment of WO2, an antibody specific for the Abeta peptides associated with Alzheimer's disease.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 438-441.  
18228239 M.Valerio, F.Porcelli, J.P.Zbilut, A.Giuliani, C.Manetti, and F.Conti (2008).
pH effects on the conformational preferences of amyloid beta-peptide (1-40) in HFIP aqueous solution by NMR spectroscopy.
  ChemMedChem, 3, 833-843.  
17534931 S.Rodziewicz-Motowidło, P.Juszczyk, A.S.Kołodziejczyk, E.Sikorska, A.Skwierawska, M.Oleszczuk, and Z.Grzonka (2007).
Conformational solution studies of the SDS micelle-bound 11-28 fragment of two Alzheimer's beta-amyloid variants (E22K and A21G) using CD, NMR, and MD techniques.
  Biopolymers, 87, 23-39.  
17215879 J.K.Rainey, L.Fliegel, and B.D.Sykes (2006).
Strategies for dealing with conformational sampling in structural calculations of flexible or kinked transmembrane peptides.
  Biochem Cell Biol, 84, 918-929.  
15649580 C.Morgan, M.Colombres, M.T.Nuñez, and N.C.Inestrosa (2004).
Structure and function of amyloid in Alzheimer's disease.
  Prog Neurobiol, 74, 323-349.  
12717720 A.Mascioni, F.Porcelli, U.Ilangovan, A.Ramamoorthy, and G.Veglia (2003).
Conformational preferences of the amylin nucleation site in SDS micelles: an NMR study.
  Biopolymers, 69, 29-41.
PDB code: 1kuw
11606220 K.Watanabe, T.Segawa, K.Nakamura, M.Kodaka, T.Konakahara, and H.Okuno (2001).
Identification of the molecular interaction site of amyloid beta peptide by using a fluorescence assay.
  J Pept Res, 58, 342-346.  
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 code is shown on the right.