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Structure paper

TitleStructural features of heteromeric channels composed of CALHM2 and CALHM4 paralogs.
Journal, issue, pagesElife, Vol. 13, Year 2024
Publish dateJun 18, 2024
AuthorsKatarzyna Drożdżyk / Martina Peter / Raimund Dutzler /
PubMed AbstractThe CALHM proteins constitute a family of large pore channels that contains six closely related paralogs in humans. Two family members, CALHM1 and 3, have been associated with the release of ATP ...The CALHM proteins constitute a family of large pore channels that contains six closely related paralogs in humans. Two family members, CALHM1 and 3, have been associated with the release of ATP during taste sensation. Both proteins form heteromeric channels that activate at positive potential and decreased extracellular Ca concentration. Although the structures of several family members displayed large oligomeric organizations of different size, their function has in most cases remained elusive. Our previous study has identified the paralogs CALHM2, 4 and, 6 to be highly expressed in the placenta and defined their structural properties as membrane proteins exhibiting features of large pore channels with unknown activation properties (Drożdżyk et al., 2020). Here, we investigated whether these placental paralogs would form heteromers and characterized heteromeric complexes consisting of CALHM2 and CALHM4 subunits using specific binders as fiducial markers. Both proteins assemble with different stoichiometries with the largest population containing CALHM2 as the predominant component. In these oligomers, the subunits segregate and reside in their preferred conformation found in homomeric channels. Our study has thus revealed the properties that govern the formation of CALHM heteromers in a process of potential relevance in a cellular context.
External linksElife / PubMed:38896440 / PubMed Central
MethodsEM (single particle)
Resolution3.07 - 3.84 Å
Structure data

19362

8rmk

EMDB-19362, PDB-8rmk:
Cryo-EM structure of human CALHM2 in complex with synthetic nanobody SbC2
Method: EM (single particle) / Resolution: 3.07 Å

19363

8rml

EMDB-19363, PDB-8rml:
Structure of heteromeric CALHM2/4 channel in complex with synthetic nanobody SbC4
Method: EM (single particle) / Resolution: 3.84 Å

19364

8rmm

EMDB-19364, PDB-8rmm:
Structure of heteromeric CALHM2/4 channel in complex with synthetic nanobodies SbC2 and SbC4
Method: EM (single particle) / Resolution: 3.26 Å

19365

8rmn

EMDB-19365, PDB-8rmn:
Cryo-EM structure of a dimer of decameric human CALHM4 in complex with synthetic nanobody SbC4
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / ion channel / large pore channels / sybody / CALHM

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