- PDB-6kku: human KCC1 structure determined in NaCl and GDN -
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基本情報
登録情報
データベース: PDB / ID: 6kku
タイトル
human KCC1 structure determined in NaCl and GDN
要素
Solute carrier family 12 member 4
キーワード
TRANSPORT PROTEIN / ion co-transporter
機能・相同性
機能・相同性情報
potassium:chloride symporter activity / Cation-coupled Chloride cotransporters / chloride ion homeostasis / potassium ion homeostasis / cell volume homeostasis / potassium ion import across plasma membrane / monoatomic ion transport / potassium ion transmembrane transport / chloride transmembrane transport / chemical synaptic transmission ...potassium:chloride symporter activity / Cation-coupled Chloride cotransporters / chloride ion homeostasis / potassium ion homeostasis / cell volume homeostasis / potassium ion import across plasma membrane / monoatomic ion transport / potassium ion transmembrane transport / chloride transmembrane transport / chemical synaptic transmission / lysosomal membrane / synapse / protein kinase binding / ATP binding / membrane / plasma membrane 類似検索 - 分子機能
ジャーナル: Science / 年: 2019 タイトル: Cryo-EM structures of the human cation-chloride cotransporter KCC1. 著者: Si Liu / Shenghai Chang / Binming Han / Lingyi Xu / Mingfeng Zhang / Cheng Zhao / Wei Yang / Feng Wang / Jingyuan Li / Eric Delpire / Sheng Ye / Xiao-Chen Bai / Jiangtao Guo / 要旨: Cation-chloride cotransporters (CCCs) mediate the coupled, electroneutral symport of cations with chloride across the plasma membrane and are vital for cell volume regulation, salt reabsorption in ...Cation-chloride cotransporters (CCCs) mediate the coupled, electroneutral symport of cations with chloride across the plasma membrane and are vital for cell volume regulation, salt reabsorption in the kidney, and γ-aminobutyric acid (GABA)-mediated modulation in neurons. Here we present cryo-electron microscopy (cryo-EM) structures of human potassium-chloride cotransporter KCC1 in potassium chloride or sodium chloride at 2.9- to 3.5-angstrom resolution. KCC1 exists as a dimer, with both extracellular and transmembrane domains involved in dimerization. The structural and functional analyses, along with computational studies, reveal one potassium site and two chloride sites in KCC1, which are all required for the ion transport activity. KCC1 adopts an inward-facing conformation, with the extracellular gate occluded. The KCC1 structures allow us to model a potential ion transport mechanism in KCCs and provide a blueprint for drug design.