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Cu2+ binding triggers αBoPrP assembly into insoluble laminar polymers
- Source :
-
FEBS Letters . Jan2004, Vol. 556 Issue 1-3, p161. 6p. - Publication Year :
- 2004
-
Abstract
- Cu2+ binding is so far the best characterized property of the prion protein. This interaction has been mapped to the N-terminal domain of the prion protein where multiple His residues occur largely embedded within the repetitive PHGGGWGQ sequence known as octarepeats. When Cu2+ interaction is studied using a solution of full-length bovine prion protein containing six octarepeats at protein concentrations above 25 μM, a drastic increase in solution turbidity is observed due to the formation of insoluble cation–protein complexes that appear as bidimensional polymer meshes. These bidimensional meshes consist of a single layer of protein molecules crosslinked by Cu2+ cations. Polymer formation is a cooperative process that proceeds by nucleation of protein molecules with a Cu2+ site occupancy of above 2. These results support the hypothesis that the N-terminal domain of prion protein is a ligand binding module that promotes crosslinked assembly, and suggest the existence of inter-repeat Cu2+ sites. [Copyright &y& Elsevier]
- Subjects :
- *COPPER
*PRIONS
*LIGANDS (Biochemistry)
Subjects
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 556
- Issue :
- 1-3
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 11826121
- Full Text :
- https://doi.org/10.1016/S0014-5793(03)01397-8