Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

The Kir2.1 potassium channel owes its inward-rectifying behavior to blocking by multivalent ions, e.g., magnesium and spermine, which access the channel from the cytoplasm and are thought to bind within the pore. To investigate the pathway followed by these ions from the cytoplasm through the pore, we have used multiscale modeling (via continuum electrostatics calculations, docking, and molecular dynamics simulations) to identify possible binding sites en route. On its way to eventually binding in the cavity, magnesium interacts extensively with Glu299, which lines the pore in the center of the intracellular domain. Interaction sites for spermine are formed by Asp255, Glu299, and Glu224. Entropic factors seem to favor interactions of spermine within the center of the cytoplasmic domain.

Original publication




Journal article



Publication Date





8758 - 8763


Animals, Computer Simulation, G Protein-Coupled Inwardly-Rectifying Potassium Channels, Humans, Ion Channel Gating, Magnesium, Mice, Models, Molecular, Potassium Channel Blockers, Potassium Channels, Inwardly Rectifying, Protein Structure, Tertiary, Spermidine, Spermine, Static Electricity, Structural Homology, Protein, Thermodynamics