title: Exploring the architecture of potassium channels using chimaeras to reveal signal transduction.
abstract: The chimeric channel, 4N/1, generated from two outwardly rectifying K+ channels by linking the N-terminal cytoplasmic domain of hKv1.4 with the transmembrane body of hKv1.1, functions as an inward rectifier. The operating range of the channel is shifted to hyperpolarizing potentials and it is inactivated at resting membrane potentials. Co-expression of a truncated form of hKv1.1 with the N-terminal domain of hKv1.4 results in the same physiology as the chimaera implying specific interactions between the two segments.
authors.affiliation: National Center for Biological Sciences, TIFR, Bangalore, India.
authors.forename: B
authors.initials: B
authors.lastname: Chanda
authors.forename: J K
authors.initials: JK
authors.lastname: Tiwari
authors.forename: A
authors.initials: A
authors.lastname: Varshney
authors.forename: M K
authors.initials: MK
authors.lastname: Mathew
mesh_terms: D000818:Animals; D004594:Electrophysiology; D015640:Ion Channel Gating; D008954:Models, Biological; D011188:Potassium / Q000378:metabolism; D015221:Potassium Channels / Q000737:chemistry* / Q000378:metabolism; D012313:RNA / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction; D014981:Xenopus
chemical_list: D015221:Potassium Channels; D011993:Recombinant Fusion Proteins; D012313:RNA; D011188:Potassium