Crystal structure and mechanism of a calcium-gated potassium channel

By Youxing Jiang, Alice Lee, Jiayun Chen, M. Cadene, Brian T. Chait, R. MacKinnon. Nature, 2002

1,355 citations recorded by the source corpus.

Subfields: Cellular and Molecular Neuroscience, Electrochemistry, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/7b7722d7eb436fd146840438df88642745acc50b

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Citations in the corpus

hERG potassium channels and cardiac arrhythmia (2006, background): “In addition, recent X-ray crystal structures of several bacterial K p channel”
hERG K(+) channels: structure, function, and clinical significance. (2012, background): “It is notable that the exon 7/8 boundary occurs at a glycine residue (Gly648 in hERG) that is one of the most highly conserved residues in all K channels (296) and defines the boundary between the upper and lower halves of the pore cavity.”
A glimpse of structural biology through X-ray crystallography. (2014, background): “Subsequent structural and biochemical studies on K+ channels uncoveredmechanistic insights into gating of the ion-conducting pore (Jiang et al., 2002, 2003; Long et al., 2005).”
Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside (2003, background): “Opening and closing channels through helix bending was also proposed for other protein”
X-ray structure of a voltage-dependent K+ channel (2003, methodology): “The gating hinge was identified when comparing the structures of KcsA (a closed K p channel) and MthK (an opened K p channel), and observing that the inner helices seem to open like the aperture of a camera by bending at a glycine residu”
The voltage-gated potassium channels and their relatives (2002, background): “But the MthK channel was a surprise: a functional channel contains eight RCK domains, one on each channel subunit and one made in a soluble form by initiation at an internal methionine of the bacterial gen”
Inwardly rectifying potassium channels: their structure, function, and physiological roles. (2010, background): “The slide helix at the cytoplasmic end of TM1 is a unique structural element of the Kir channel family compared with other K channels (143, 336, 338, 404, 466) (Fig.”