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A potential molecular switch in an alpha-helical coiled coil
Charles A Laughton1, Ben F Luisi, J Venkatesh Pratap
1School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, United Kingdom.
The GCN4 protein
Area of Science:
- Molecular Biology
- Biophysics
- Structural Biology
Background:
- The yeast DNA-binding protein GCN4 is a homo-dimer.
- It forms a self-complementary coiled-coil interface.
Purpose of the Study:
- To investigate the potential bistability of coiled-coil interfaces.
- To explore the switching mechanism between states in the GCN4 coiled coil.
Main Methods:
- Utilized Molecular Dynamics (MD) computations.
- Analyzed the GCN4 coiled-coil structure and dynamics.
Main Results:
- Demonstrated that the GCN4 coiled coil can switch between two states.
- Identified a pathway involving progressive 'flipping' of steps along the interface.
Conclusions:
- Coiled-coil interfaces can exhibit bistability.
- This bistability has implications for allosteric signal transmission in homo-dimers.
- Potential relevance to helix packing in globular proteins.
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