Related Experiment Videos
Cu2+ binding triggers alphaBoPrP assembly into insoluble laminar polymers
Reinerio González-Iglesias1, Gema Elvira, José A Rodríguez-Navarro
1Instituto Química-Física 'Rocasolano', CSIC, Serrano 119, E-28006, Madrid, Spain.
FEBS Letters
|January 7, 2004
Summary
Copper (Cu2+) binding to prion protein
Area of Science:
- Biochemistry
- Structural Biology
- Neuroscience
Background:
- Copper (Cu2+) binding is a key property of the prion protein.
- This interaction occurs in the N-terminal domain, specifically within the octarepeat sequences (PHGGGWGQ).
Purpose of the Study:
- To investigate the structural consequences of Cu2+ binding to full-length bovine prion protein.
- To understand the mechanism of prion protein assembly induced by Cu2+.
Main Methods:
- Studying full-length bovine prion protein with six octarepeats.
- Utilizing protein concentrations above 25 microM in solution.
- Observing solution turbidity changes and complex formation.
Main Results:
- High concentrations of Cu2+ induce insoluble cation-protein complexes.
- These complexes form bidimensional polymer meshes of a single protein layer crosslinked by Cu2+.
- Polymer formation is a cooperative process initiated by nucleation at a Cu2+ site occupancy above 2.
Conclusions:
- The N-terminal domain of prion protein acts as a ligand-binding module promoting crosslinked assembly.
- Inter-repeat Cu2+ binding sites likely exist within the prion protein structure.