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Structure paper

TitleAmyloid precursor protein dimerization and synaptogenic function depend on copper binding to the growth factor-like domain
Journal, issue, pagesJ. Neurosci., Vol. 34, Page 11159-11172, Year 2014
Publish dateFeb 28, 2013 (structure data deposition date)
AuthorsBaumkotter, F. / Schmidt, N. / Vargas, C. / Schilling, S. / Weber, R. / Wagner, K. / Fiedler, S. / Klug, W. / Radzimanowski, J. / Nickolaus, S. ...Baumkotter, F. / Schmidt, N. / Vargas, C. / Schilling, S. / Weber, R. / Wagner, K. / Fiedler, S. / Klug, W. / Radzimanowski, J. / Nickolaus, S. / Keller, S. / Eggert, S. / Wild, K. / Kins, S.
External linksJ. Neurosci. / PubMed:25122912
MethodsX-ray diffraction
Resolution1.75 Å
Structure data

PDB-4jfn:
Crystal structure of the N-terminal, growth factor-like domain of the amyloid precursor protein bound to copper
Method: X-RAY DIFFRACTION / Resolution: 1.75 Å

Chemicals

ChemComp-CU:
COPPER (II) ION

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsMETAL BINDING PROTEIN / Alzheimer's disease / GFLD / APP / Growth factor-like domain / copper binding

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