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We recently examined how Kir1.1, an inwardly-rectifying potassium channel that is found in the kidneys, opens and closes in response to being stimulated by changes in pH or the presence of absence of PIP2, a signalling lipid [BIBCITE%%0%]. The key result of that paper was that we could identify several networks of residues that came together to form one large gate when the channel was open. In this addendum paper, we examine how mutating several of these residues affected the kinetics of gating [BIBCITE%%1%]. By comparing the on- and off-rates we are able to infer that the transition state more closely resembles that pre-open, rather than open, state. This paper is open access and is freely available to download.
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