6PZT

cryo-EM structure of human NKCC1

6PZT の概要

• エントリーDOI: 10.2210/pdb6pzt/pdb
• EMDBエントリー: 20537
• 分子名称: Solute carrier family 12 member 2 (1 entity in total)
• 機能のキーワード: nkcc1, 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: 263336.97

構造登録者

Cao, E.,Wang, Q.,Yang, X. (登録日: 2019-08-01, 公開日: 2020-03-25, 最終更新日: 2024-10-23)

主引用文献

Yang, X.,Wang, Q.,Cao, E.
Structure of the human cation-chloride cotransporter NKCC1 determined by single-particle electron cryo-microscopy.
Nat Commun, 11:1016-1016, 2020

PubMed Abstract: The secondary active cation-chloride cotransporters (CCCs) utilize the existing Na and/or K gradients to move Cl into or out of cells. NKCC1 is an intensively studied member of the CCC family and plays fundamental roles in regulating trans-epithelial ion movement, cell volume, chloride homeostasis and neuronal excitability. Here, we report a cryo-EM structure of human NKCC1 captured in a partially loaded, inward-open state. NKCC1 assembles into a dimer, with the first ten transmembrane (TM) helices harboring the transport core and TM11-TM12 helices lining the dimer interface. TM1 and TM6 helices break α-helical geometry halfway across the lipid bilayer where ion binding sites are organized around these discontinuous regions. NKCC1 may harbor multiple extracellular entryways and intracellular exits, raising the possibility that K, Na, and Cl ions may traverse along their own routes for translocation. NKCC1 structure provides a blueprint for further probing structure-function relationships of NKCC1 and other CCCs.

PubMed: 32081947
DOI: 10.1038/s41467-020-14790-3

実験手法

ELECTRON MICROSCOPY (3.46 Å)