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6KKU

human KCC1 structure determined in NaCl and GDN

6KKU の概要
エントリーDOI10.2210/pdb6kku/pdb
EMDBエントリー0701 0702 0703
関連するBIRD辞書のPRD_IDPRD_900018
分子名称Solute carrier family 12 member 4, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, ... (5 entities in total)
機能のキーワードion co-transporter, transport protein
由来する生物種Homo sapiens (Human)
タンパク質・核酸の鎖数2
化学式量合計248280.95
構造登録者
Liu, S.,Chang, S.,Ye, S.,Bai, X.,Guo, J. (登録日: 2019-07-27, 公開日: 2019-10-23, 最終更新日: 2025-07-02)
主引用文献Liu, S.,Chang, S.,Han, B.,Xu, L.,Zhang, M.,Zhao, C.,Yang, W.,Wang, F.,Li, J.,Delpire, E.,Ye, S.,Bai, X.C.,Guo, J.
Cryo-EM structures of the human cation-chloride cotransporter KCC1.
Science, 366:505-508, 2019
Cited by
PubMed Abstract: 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.
PubMed: 31649201
DOI: 10.1126/science.aay3129
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.5 Å)
構造検証レポート
Validation report summary of 6kku
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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