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TitleStructural insight into the allosteric inhibition of human sodium-calcium exchanger NCX1 by XIP and SEA0400.
Journal, issue, pagesEMBO J, Vol. 43, Issue 1, Page 14-31, Year 2024
Publish dateDec 15, 2023
AuthorsYanli Dong / Zhuoya Yu / Yue Li / Bo Huang / Qinru Bai / Yiwei Gao / Qihao Chen / Na Li / Lingli He / Yan Zhao /
PubMed AbstractSodium-calcium exchanger proteins influence calcium homeostasis in many cell types and participate in a wide range of physiological and pathological processes. Here, we elucidate the cryo-EM ...Sodium-calcium exchanger proteins influence calcium homeostasis in many cell types and participate in a wide range of physiological and pathological processes. Here, we elucidate the cryo-EM structure of the human Na/Ca exchanger NCX1.3 in the presence of a specific inhibitor, SEA0400. Conserved ion-coordinating residues are exposed on the cytoplasmic face of NCX1.3, indicating that the observed structure is stabilized in an inward-facing conformation. We show how regulatory calcium-binding domains (CBDs) assemble with the ion-translocation transmembrane domain (TMD). The exchanger-inhibitory peptide (XIP) is trapped within a groove between the TMD and CBD2 and predicted to clash with gating helices TMs at the outward-facing state, thus hindering conformational transition and promoting inactivation of the transporter. A bound SEA0400 molecule stiffens helix TM2ab and affects conformational rearrangements of TM2ab that are associated with the ion-exchange reaction, thus allosterically attenuating Ca-uptake activity of NCX1.3.
External linksEMBO J / PubMed:38177313 / PubMed Central
MethodsEM (single particle)
Resolution3.5 Å
Structure data

36465

8jp0

EMDB-36465, PDB-8jp0:
structure of human sodium-calciumexchanger NCX1
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-EKY:
2-{4-[(2,5-difluorophenyl)methoxy]phenoxy}-5-ethoxyaniline

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / sodium/calcium exchanger / membrane protein

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