6VW9

C-terminal regulatory domain of the chloride transporter KCC-1 from C. elegans, proteolyzed during crystallization

6VW9 の概要

• エントリーDOI: 10.2210/pdb6vw9/pdb
• 分子名称: K+/Cl-Cotransporter, 3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: cation-chloride-cotransporter, slc transporter, cytosolic domain, transport protein
• 由来する生物種: Caenorhabditis elegans; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35152.83

構造登録者

Zimanyi, C.M.,Cheung, J. (登録日: 2020-02-19, 公開日: 2020-07-15, 最終更新日: 2024-03-06)

主引用文献

Zimanyi, C.M.,Guo, M.,Mahmood, A.,Hendrickson, W.A.,Hirsh, D.,Cheung, J.
Structure of the Regulatory Cytosolic Domain of a Eukaryotic Potassium-Chloride Cotransporter.
Structure, 28:1051-1060.e4, 2020

PubMed Abstract: Cation-chloride cotransporters (CCCs) regulate the movement of chloride across membranes, controlling physiological processes from cell volume maintenance to neuronal signaling. Human CCCs are clinical targets for existing diuretics and potentially additional indications. Here, we report the X-ray crystal structure of the soluble C-terminal regulatory domain of a eukaryotic potassium-chloride cotransporter, Caenorhabditis elegans KCC-1. We observe a core α/β fold conserved among CCCs. Using structure-based sequence alignment, we analyze similarities and differences to the C-terminal domains of other CCC family members. We find that important regulatory motifs are in less-structured regions and residues important for dimerization are not widely conserved, suggesting that oligomerization and its effects may vary within the larger family. This snapshot of a eukaryotic KCC is a valuable starting point for the rational design of studies of cellular chloride regulation.

PubMed: 32679039
DOI: 10.1016/j.str.2020.06.009

実験手法

X-RAY DIFFRACTION (1.8 Å)