7D10

Human NKCC1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.52 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.1 of the entry. See complete history


Literature

The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.

Zhang, S.Zhou, J.Zhang, Y.Liu, T.Friedel, P.Zhuo, W.Somasekharan, S.Roy, K.Zhang, L.Liu, Y.Meng, X.Deng, H.Zeng, W.Li, G.Forbush, B.Yang, M.

(2021) Commun Biol 4: 226-226

  • DOI: https://doi.org/10.1038/s42003-021-01750-w
  • Primary Citation of Related Structures:  
    7D10, 7D14

  • PubMed Abstract: 

    NKCC and KCC transporters mediate coupled transport of Na + +K + +Cl - and K + +Cl - across the plasma membrane, thus regulating cell Cl - concentration and cell volume and playing critical roles in transepithelial salt and water transport and in neuronal excitability. The function of these transporters has been intensively studied, but a mechanistic understanding has awaited structural studies of the transporters. Here, we present the cryo-electron microscopy (cryo-EM) structures of the two neuronal cation-chloride cotransporters human NKCC1 (SLC12A2) and mouse KCC2 (SLC12A5), along with computational analysis and functional characterization. These structures highlight essential residues in ion transport and allow us to propose mechanisms by which phosphorylation regulates transport activity.


  • Organizational Affiliation

    Ministry of Education Key Laboratory of Protein Science, Tsinghua-Peking Center for Life Sciences, Beijing Advanced Innovation Center for Structural Biology, School of Life Sciences, Tsinghua University, Beijing, China.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Solute carrier family 12 member 2
A, B
1,212Homo sapiensMutation(s): 0 
Gene Names: SLC12A2NKCC1
Membrane Entity: Yes 
UniProt & NIH Common Fund Data Resources
Find proteins for P55011 (Homo sapiens)
Explore P55011 
Go to UniProtKB:  P55011
PHAROS:  P55011
GTEx:  ENSG00000064651 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP55011
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.52 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2021-04-14
    Type: Initial release
  • Version 1.1: 2024-05-29
    Changes: Data collection, Database references