The open pore conformation of potassium channels

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Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “The arrangement of the helices to form the transmembrane domain shares significant similarity with that of other K channel families including a bacterial channel KcsA (143, 539, 894), a bacterial calcium-activated channel MthK (336, 337), a bacterial voltage-gated channel KvAP (338), and a mammalian”
Structure of a complex between a voltage-gated calcium channel β-subunit and an α-subunit domain (2004, background): “Motions of pore-lining transmembrane segments are a common theme emerging in ion channel gatin”
X-ray structure of a voltage-dependent K+ channel (2003, background): “This glycine is conserved at a specific location in the inner helix of many K p channels, including KvAP, and has been proposed to underlie gatin”
Glutamate Receptor Ion Channels: Structure, Regulation, and Function (2010, background): “However, given that glutamate receptors lack a glycine hinge within their M3 transmembrane helix, a structural element proposed to be essential for K channel opening (Doyle et al., 1998; Jiang et al., 2002), there will be differences in detail of how the conformational changes in M3 occur.”
KATP channels as molecular sensors of cellular metabolism (2006, background): “Crystallization of the bacterial MthK K p channel in an apparently open state led to a now widely accepted hypothesi”