I collaborate with Prof. Henry Sackin in modeling point mutations in inwardly-rectifying potassium channels.
Sackin H, Nanazashvili M, Li H, Palmer LG, Walters DE. A conserved arginine near the filter of Kir1.1 controls Rb/K selectivity. Channels, 4:203-214 (2010).
Sackin H, Nanazashvili M, Li H, Palmer LG, Walters DE. An inter-subunit salt bridge near the selectivity filter stabilizes the active state of Kir1.1. Biophys. J. 97, 1058 - 1066, 2009. PMCID: PMC2726312
Sackin H, Nanazashvili M, Li H, Palmer LG, Walters DE. External K activation of Kir1.1 depends on the pH gate. Biophys. J. 93:L14-L16 (2007).
Sackin H, Nanazashvili M, Palmer LG, Krambis M, Walters DE. Structural locus of the pH gate in the Kir1.1 inward rectifier channel. Biophys. J. 88:2597-2606 (2005).
Sackin H, Syn S, Palmer LG, Choe H, Walters DE. Regulation of ROMK by extracellular cations. Biophys. J. 80:683-697 (2001).
This page uses the Jmol java applet. Be sure your browser is java-enabled. Be patient--it may take several seconds for the structure to load! After it loads, you can drag the structure to rotate it or shift-drag to zoom. If you have a 2-button or 3-button mouse, the right-button may give you more display options.
Kir1.1, homology-modeled on the bacterial K+ channel structure 1P7B. The channel is composed of four identical protein chains, represented as backbone ribbons. Four potassium ions (red spheres) are located in the selectivity filter of the channel.
© by D. Eric Walters