KcsA is a K+ channel protein from a bacterium called Streptomyces lividans. Based on work of Rod MacKinnon (Doyle et al., 1998. Science 280: 69-77), a co-recipient of the 2003 Nobel Prize in Chemistry, we know that KscA has a three-dimensional structure that is very similar to human K+ channels that mediate vital functions of the nervous system. This channel protein has an exquisite mechanism of ionic selectivity, preferring inorganic cations such as K+, Rb+, and Tl+ over slightly smaller ions such as Na+ and Li+. We have recently developed a new approach to measuring ion-channel interactions of KcsA based on the use of gel electrophoresis (SDS-PAGE) to monitor the stability of the channel tetramer in the presence of different ions. We are currently using this approach to measure the binding affinity of KscA for different inorganic cations and plan to extend this technique to other types of K+ channels.

This website was created by Melissa Bell, Lindsay Schwarting, and Niall Mangan. Updates by Niall Mangan. All information and images on this site are ©Clarkson University Laboratory of Molecular Neuroscience.