7D10

Human NKCC1

Summary for 7D10

• Entry DOI: 10.2210/pdb7d10/pdb
• EMDB information: 30542
• Descriptor: Solute carrier family 12 member 2, PALMITIC ACID (2 entities in total)
• Functional Keywords: membrane protein, transporter
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 264192.54

Authors

Zhang, S.,Yang, M. (deposition date: 2020-09-12, release date: 2021-04-14, Last modification date: 2024-05-29)

Primary citation

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.
The structural basis of function and regulation of neuronal cotransporters NKCC1 and KCC2.
Commun Biol, 4:226-226, 2021

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.

PubMed: 33597714
DOI: 10.1038/s42003-021-01750-w

Experimental method

ELECTRON MICROSCOPY (3.52 Å)