Abstract
Gating mechanism is one of the most important problems in the study on ion channels. Despite the important achievement of the high-resolution structures of several K+ channels, the gating mechanism underlie the conformational change is still unclear. Here we employ the all-atom simulation method to study the gating ring of Mthk, a Ca2+-activated K+ channel, with a long time of 2 µs. we find two kinds of important Ca2+ binding sites. One plays a significant role in the stabilization of RCK structure; another one may participate in the conformational change of the gating ring structure and have a direct relation with the mechanism of gating. Morever, two arginines R132, R135 nearby the Ca2+ binding site E133, E258,E259 play a key role the process of conformational change.
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