Systematic analyses of structure/function variability of viral K+ channels for the development of synthetic channels

Small viral potassium (K+) channels represent with less than 100 amino acids (aa) per monomer the pore module of every K+ channel. The combination small size and robust function makes them ideal model systems to investigate basic structure/function correlations in channel pores. In prototype KcvPBCV-1 second TM helix ends C-terminus which last aa L94 plays an important role gating. A salt bridge network between free negative charge carboxyl group positively charged N-terminus determine opening closing.