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-Structure paper
タイトル | Cryo-EM structures of the human cation-chloride cotransporter KCC1. |
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ジャーナル・号・ページ | Science, Vol. 366, Issue 6464, Page 505-508, Year 2019 |
掲載日 | 2019年10月25日 |
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 / |
PubMed 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. |
リンク | Science / PubMed:31649201 |
手法 | EM (単粒子) |
解像度 | 2.9 - 3.5 Å |
構造データ | EMDB-0701, PDB-6kkr: |
化合物 | ChemComp-CL: ChemComp-K: ChemComp-DU0: |
由来 |
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キーワード | TRANSPORT PROTEIN / ion co-transporter |