Cryo-EM structure of human KCC1 bound with inhibitor VU0463271
Ontology highlight
ABSTRACT:
SUBMITTER: Yongxiang Zhao
PROVIDER: EMPIAR-11047 | biostudies-other |
REPOSITORIES: biostudies-other
Publications
Structure of the human cation-chloride cotransport KCC1 in an outward-open state.
Zhao Yongxiang Y Shen Jiemin J Wang Qinzhe Q Ruiz Munevar Manuel Jose MJ Vidossich Pietro P De Vivo Marco M Zhou Ming M Cao Erhu E
Proceedings of the National Academy of Sciences of the United States of America 20220627 27
Cation-chloride cotransporters (CCCs) catalyze electroneutral symport of Cl<sup>-</sup> with Na<sup>+</sup> and/or K<sup>+</sup> across membranes. CCCs are fundamental in cell volume homeostasis, transepithelia ion movement, maintenance of intracellular Cl<sup>-</sup> concentration, and neuronal excitability. Here, we present a cryoelectron microscopy structure of human K<sup>+</sup>-Cl<sup>-</sup> cotransporter (KCC)1 bound with the VU0463271 inhibitor in an outward-open state. In contrast to m ...[more]
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