• pore
  • Chloroquine interacts with acidic residues (mainly Glu224 and Glu299) lining the cytoplasmic pore of the channel. (aspetjournals.org)
  • In tetrameric Kv channels, each of the four subunits contain six transmembrane helices (S1-S6), with the S5-S6 forming the centrally located pore domain, and the S1-S4 helices forming each of four voltage-sensing domains. (rupress.org)
  • KCNJ11 forms the channel pore while ABCC9 is required for activation and regulation (By similarity). (uniprot.org)
  • inhibitor
  • The data strongly suggest that tamoxifen, its metabolite, and the estrogen receptor inhibitor raloxifene inhibit Kir2.x channels indirectly by interfering with the interaction between the channel and PIP 2 . (aspetjournals.org)
  • Chimeras in which S3b-S4 paddle motifs are transferred between Kv2.1 and Shaker Kv channels, as well as experiments with the related tarantula toxin GxTx-1E, lead us to conclude that the actions of tarantula toxins are not simply a product of where they bind to the channel, but that fine structural details of the toxin-channel interface determine whether a toxin is an inhibitor or opener. (rupress.org)
  • properties
  • In this study we identify residues at an intersubunit interface between the cytoplasmic domains of Kir5.1 and Kir4.1 that influence the novel rectification and gating properties of heteromeric Kir4.1/Kir5.1 channels and that also contribute to their pH sensitivity. (ox.ac.uk)
  • range
  • Potassium channels are present in most mammalian cells, where they participate in a wide range of physiologic responses. (nih.gov)
  • These novel channels are also inhibited by intracellular pH within the physiological range and are thought to play a key role in linking K+ and H+ homeostasis by the kidney. (ox.ac.uk)
  • Using a range of previously characterized mutants of the Shaker Kv channel, we find that hanatoxin stabilizes an activated conformation of the voltage sensors, in addition to promoting opening through an effect on the final opening transition. (rupress.org)
  • Voltage-activated ion channels play a wide range of critical roles in electrical and chemical signaling within biological systems. (rupress.org)