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TitleStructure and mechanism of the human NHE1-CHP1 complex.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 3474, Year 2021
Publish dateJun 9, 2021
AuthorsYanli Dong / Yiwei Gao / Alina Ilie / DuSik Kim / Annie Boucher / Bin Li / Xuejun C Zhang / John Orlowski / Yan Zhao /
PubMed AbstractSodium/proton exchanger 1 (NHE1) is an electroneutral secondary active transporter present on the plasma membrane of most mammalian cells and plays critical roles in regulating intracellular pH and ...Sodium/proton exchanger 1 (NHE1) is an electroneutral secondary active transporter present on the plasma membrane of most mammalian cells and plays critical roles in regulating intracellular pH and volume homeostasis. Calcineurin B-homologous protein 1 (CHP1) is an obligate binding partner that promotes NHE1 biosynthetic maturation, cell surface expression and pH-sensitivity. Dysfunctions of either protein are associated with neurological disorders. Here, we elucidate structures of the human NHE1-CHP1 complex in both inward- and inhibitor (cariporide)-bound outward-facing conformations. We find that NHE1 assembles as a symmetrical homodimer, with each subunit undergoing an elevator-like conformational change during cation exchange. The cryo-EM map reveals the binding site for the NHE1 inhibitor cariporide, illustrating how inhibitors block transport activity. The CHP1 molecule differentially associates with these two conformational states of each NHE1 monomer, and this association difference probably underlies the regulation of NHE1 pH-sensitivity by CHP1.
External linksNat Commun / PubMed:34108458 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.5 Å
Structure data

30847

7dsv

EMDB-30847, PDB-7dsv:
Structure of a human NHE1-CHP1 complex under pH 6.5
Method: EM (single particle) / Resolution: 3.4 Å

30848

7dsw

EMDB-30848, PDB-7dsw:
Structure of a human NHE1-CHP1 complex under pH 7.5
Method: EM (single particle) / Resolution: 3.3 Å

30849

7dsx

EMDB-30849, PDB-7dsx:
Structure of a human NHE1-CHP1 complex under pH 7.5, bound by cariporide
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM / POPC

ChemComp-PGT:
(1S)-2-{[{[(2R)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE / phospholipid*YM / Phosphatidylglycerol

ChemComp-HG0:
N-[bis(azanyl)methylidene]-3-methylsulfonyl-4-propan-2-yl-benzamide / inhibitor*YM / Cariporide

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Transporter

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