6KKU
human KCC1 structure determined in NaCl and GDN
6KKU の概要
| エントリーDOI | 10.2210/pdb6kku/pdb |
| EMDBエントリー | 0701 0702 0703 |
| 関連するBIRD辞書のPRD_ID | PRD_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 | |
| 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: 31649201DOI: 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) |
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