Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein

@article{Rossjohn1999CrystalSO,
  title={Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein},
  author={Jamie Rossjohn and Roberto Cappai and Susanne C. Feil and Anna Henry and William J McKinstry and Denise Galatis and Lars Hesse and Gerd Multhaup and Konrad T. Beyreuther and Colin L. Masters and Michael W. Parker},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={327-331}
}
Amyloid precursor protein (APP) plays a central role in Alzheimer disease. A proteolytic-breakdown product of APP, called β-amyloid, is a major component of the diffuse and fibrillar deposits found in Alzheimer diseased brains. The normal physiological role of APP remains largely unknown despite much work. A knowledge of its function will not only provide insights into the genesis of the disease but may also prove vital in the development of an effective therapy. Here we describe the 1.8… 
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238 Citations

Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein.
TLDR
An independently folded extracellular domain of human APP localized proximal to the Abeta sequence is identified, and the three-dimensional structure of this domain is determined by NMR spectroscopy.
Solution studies and structural model of the extracellular domain of the human amyloid precursor protein.
Folding and Stability of the Extracellular Domain of the Human Amyloid Precursor Protein*
TLDR
The relatively low stability of the native state of sAPPα suggests that conformational plasticity may play a role in allowing APP to interact with a number of distinct physiological ligands.
Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein
TLDR
The APP-based signal transduction, cell–cell- and/or cell–ECM interaction should depend on dimerization induced by heparin, as well as on pH, arguing that APP could fulfill different functions depending on its (sub)cellular localization.
The structural biology of the amyloid precursor protein APP – a complex puzzle reveals its multi-domain architecture
TLDR
Current understanding of the structure-function-relationship of the multi-domain protein APP, which consists of the two folded E1 and E2 segments that are connected to one another and to the single transmembrane helix by flexible segments, is summarized.
The amyloid precursor protein and its homologues: structural and functional aspects of native and pathogenic oligomerization.
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.
Structural studies of the Alzheimer's amyloid precursor protein copper-binding domain reveal how it binds copper ions.
The amyloid precursor protein shows a pH-dependent conformational switch in its E1 domain.
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References

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TLDR
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TLDR
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TLDR
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TLDR
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TLDR
A role for Fe65 in the pathogenesis of familial Alzheimer's disease is suggested by the finding that mutant APP shows an altered in vivo interaction with Fe65, as demonstrated by anti-Fe65 co-immunoprecipitation experiments.
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TLDR
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