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- Title
Cu<sup>2+</sup> binding triggers αBoPrP assembly into insoluble laminar polymers
- Authors
González-Iglesias, Reinerio; Elvira, Gema; Rodríguez-Navarro, José A.; Vélez, Marisela; Calero, Miguel; Pajares, María A.; Gasset, María
- 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.
- Subjects
COPPER; PRIONS; LIGANDS (Biochemistry)
- Publication
FEBS Letters, 2004, Vol 556, Issue 1-3, p161
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/S0014-5793(03)01397-8