Potassium channel structure: domain by domain

Since the determination of the structure of a bacterial potassium channel, the ion channel community has managed to gain momentum in the quest for a c omplete picture. The information is coming at a steady flow, on a domain by domain basis. Recent discoveries are starting to reveal clues to the compl ex manner in which potassium channels show enormous diversity of function a nd also to their methods of regulation. Currently, the structures of four d omains are known, with the most recent addition being the KVP structure. As efforts continue in the study of the transmembrane domains, especially the voltage-sensing apparatus, there has been a new realization with respect t o the identification and role of the cytoplasmic domains in protein-protein interactions in particular. An additional discovery, considerably aided by recent genomic analysis, is that potassium channels comprising subunits wi th two pore region's and four transmembrane helices combined in a dimeric f ashion are abundant and are probable targets for local anesthetics.