8ste

From Proteopedia
Revision as of 10:05, 18 May 2023 by OCA (talk | contribs) (New page: ==Cryo-EM structure of NKCC1 Fu_CTD== <StructureSection load='8ste' size='340' side='right'caption='8ste, resolution 3.34Å' scene=''> == Structural highlights == ...)
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search

Cryo-EM structure of NKCC1 Fu_CTDCryo-EM structure of NKCC1 Fu_CTD

Structural highlights

8ste is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

A0A8C9GPS0_9PRIM

Publication Abstract from PubMed

The Na-K-2Cl cotransporter-1 (NKCC1) is an electroneutral Na(+)-dependent transporter responsible for simultaneously translocating Na(+), K(+), and Cl(-) ions into cells. In human tissue, NKCC1 plays a critical role in regulating cytoplasmic volume, fluid intake, chloride homeostasis, and cell polarity. Here, we report four structures of human NKCC1 (hNKCC1), both in the absence and presence of loop diuretic (bumetanide or furosemide), using single-particle cryo-electron microscopy. These structures allow us to directly observe various novel conformations of the hNKCC1 dimer. They also reveal two drug-binding sites located at the transmembrane and cytosolic carboxyl-terminal domains, respectively. Together, our findings enable us to delineate an inhibition mechanism that involves a coupled movement between the cytosolic and transmembrane domains of hNKCC1.

Inhibition mechanism of NKCC1 involves the carboxyl terminus and long-range conformational coupling.,Moseng MA, Su CC, Rios K, Cui M, Lyu M, Glaza P, Klenotic PA, Delpire E, Yu EW Sci Adv. 2022 Oct 28;8(43):eabq0952. doi: 10.1126/sciadv.abq0952. Epub 2022 Oct , 28. PMID:36306358[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Moseng MA, Su CC, Rios K, Cui M, Lyu M, Glaza P, Klenotic PA, Delpire E, Yu EW. Inhibition mechanism of NKCC1 involves the carboxyl terminus and long-range conformational coupling. Sci Adv. 2022 Oct 28;8(43):eabq0952. PMID:36306358 doi:10.1126/sciadv.abq0952

8ste, resolution 3.34Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA