タンパク質・ペプチド: Isoform J of Calcium-activated potassium channel slowpoke
リガンド: MAGNESIUM ION
リガンド: POTASSIUM ION
キーワード
Potassium transport / BK channel / TRANSPORT PROTEIN
機能・相同性
機能・相同性情報
Sperm Motility And Taxes / negative regulation of neuromuscular synaptic transmission / regulation of synaptic assembly at neuromuscular junction / male courtship behavior, veined wing generated song production / large conductance calcium-activated potassium channel activity / calcium-activated potassium channel activity / circadian behavior / monoatomic ion channel complex / potassium ion transmembrane transport / potassium ion transport ...Sperm Motility And Taxes / negative regulation of neuromuscular synaptic transmission / regulation of synaptic assembly at neuromuscular junction / male courtship behavior, veined wing generated song production / large conductance calcium-activated potassium channel activity / calcium-activated potassium channel activity / circadian behavior / monoatomic ion channel complex / potassium ion transmembrane transport / potassium ion transport / circadian rhythm / postsynaptic membrane / neuron projection / response to xenobiotic stimulus / neuronal cell body / membrane / plasma membrane 類似検索 - 分子機能
: / Ca2+-activated K+ channel Slowpoke, TrkA_C like domain / : / Calcium-activated potassium channel BK, alpha subunit / Calcium-activated BK potassium channel alpha subunit / RCK N-terminal domain profile. / Ion transport domain / Ion transport protein / NAD(P)-binding domain superfamily 類似検索 - ドメイン・相同性
ジャーナル: Nat Commun / 年: 2021 タイトル: Small molecule modulation of the Drosophila Slo channel elucidated by cryo-EM. 著者: Tobias Raisch / Andreas Brockmann / Ulrich Ebbinghaus-Kintscher / Jörg Freigang / Oliver Gutbrod / Jan Kubicek / Barbara Maertens / Oliver Hofnagel / Stefan Raunser / 要旨: Slowpoke (Slo) potassium channels display extraordinarily high conductance, are synergistically activated by a positive transmembrane potential and high intracellular Ca concentrations and are ...Slowpoke (Slo) potassium channels display extraordinarily high conductance, are synergistically activated by a positive transmembrane potential and high intracellular Ca concentrations and are important targets for insecticides and antiparasitic drugs. However, it is unknown how these compounds modulate ion translocation and whether there are insect-specific binding pockets. Here, we report structures of Drosophila Slo in the Ca-bound and Ca-free form and in complex with the fungal neurotoxin verruculogen and the anthelmintic drug emodepside. Whereas the architecture and gating mechanism of Slo channels are conserved, potential insect-specific binding pockets exist. Verruculogen inhibits K transport by blocking the Ca-induced activation signal and precludes K from entering the selectivity filter. Emodepside decreases the conductance by suboptimal K coordination and uncouples ion gating from Ca and voltage sensing. Our results expand the mechanistic understanding of Slo regulation and lay the foundation for the rational design of regulators of Slo and other voltage-gated ion channels.