Gating rings formed by RCK domains: keys to gate opening.
Lingle
Christopher J
CJ
Department of Anesthesiology, Washington University School of Medicine, MO 63105, USA. clingle@morpheus.wustl.edu
D000494:Allosteric Regulation; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D002118:Calcium / Q000378:metabolism; D027682:Cation Transport Proteins / Q000378:metabolism; D051668:Delayed Rectifier Potassium Channels / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D015640:Ion Channel Gating; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D024681:Potassium Channels, Calcium-Activated / Q000737:chemistry / Q000378:metabolism*; D024661:Potassium Channels, Inwardly Rectifying / Q000737:chemistry / Q000378:metabolism*; D011487:Protein Conformation; D021122:Protein Subunits
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D027682:Cation Transport Proteins; D051668:Delayed Rectifier Potassium Channels; C113206:KtrB protein, Bacteria; D008565:Membrane Proteins; D024681:Potassium Channels, Calcium-Activated; D024661:Potassium Channels, Inwardly Rectifying; D021122:Protein Subunits; D002118:Calcium