Potassium channels: life in the post-structural world.
More than three years have passed since the first structure of a potassium channel protein revealed fundamental molecular details of a platform for ion-selective conduction. Recent efforts have turned to understanding what this structure tells us about potassium channel structure and function in general and, most importantly, which questions remain unanswered. Successes in solving membrane protein structures are still hard won and slow. High-resolution studies of cytoplasmic channel domains and channel-associated proteins, the most tractable entry points for dissecting large, complex eukaryotic channels, are revealing a modularity of function commonly seen in many other biological systems. Studies of these domains bring into sharp focus issues of channel regulation, how these domains and associated proteins are coupled to the transmembrane domains to influence channel function, and how ion channels are integrated into cellular signaling pathways.
Minor
D L
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Department of Biochemistry and Biophysics, Cardiovascular Research Institute, 513 Parnassus Avenue, HSE 1308, Box 0130, University of California, San Francisco, 94143-0130, USA. minor@itsa.ucsf.edu
D000595:Amino Acid Sequence; D001419:Bacteria / Q000737:chemistry; D001692:Biological Transport; D017124:Conserved Sequence; D015640:Ion Channel Gating / Q000502:physiology; D008958:Models, Molecular; D009154:Mutation; D015221:Potassium Channels / Q000737:chemistry* / Q000235:genetics / Q000502:physiology*; D011487:Protein Conformation; D016415:Sequence Alignment
D015221:Potassium Channels