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Structure paper

TitleMolecular architecture of the human TRPC1/C5 heteromeric channel.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Page 317, Year 2025
Publish dateDec 10, 2025
AuthorsSun-Hong Kim / Hyunwoo Park / Jinhyeong Kim / Hana Kang / Jongdae Won / Byoung-Cheol Lee / Insuk So / Hyung Ho Lee /
PubMed AbstractTransient receptor potential (TRP) ion channels form heteromers through combinatorial associations of distinct subunits, contributing to the diversity of TRP channel functions. Among them, TRPC5, ...Transient receptor potential (TRP) ion channels form heteromers through combinatorial associations of distinct subunits, contributing to the diversity of TRP channel functions. Among them, TRPC5, which forms a heteromer with TRPC1, represents an attractive pharmaceutical target for treating anxiety and depression. Here, we present the cryo-electron microscopy structure of the human TRPC1/C5 heteromer, composed of one TRPC1 subunit and three TRPC5 subunits. The incorporation of TRPC1 into the heteromer disrupts the C symmetry of the TRPC5 homotetramer, resulting in a distinct ion conduction pathway characterized by an asymmetrically constricted selectivity filter and an asymmetric lower gate. The TRPC1/C5 heteromer displays recognizable structural features compared to the TRPC1/C4 heteromer, including a noncanonically tilted coiled-coil domain and a distinct intersubunit interactions. Furthermore, we elucidate the structures of human TRPC5 bound to the TRPC1/4/5-specific agonist, (-)-Englerin A. Our findings establish a foundation for exploring the diversity of heteromeric TRP channels and pave the way for targeting TRPC1/C5 as a therapeutic strategy.
External linksNat Commun / PubMed:41372144 / PubMed Central
MethodsEM (single particle)
Resolution2.43 - 3.03 Å
Structure data

62343

9khi

EMDB-62343, PDB-9khi:
Cryo-EM structure of heteromeric TRPC channel
Method: EM (single particle) / Resolution: 2.7 Å

62344

9khj

EMDB-62344, PDB-9khj:
Cryo-EM structure of homomeric TRPC channel, class 1
Method: EM (single particle) / Resolution: 2.62 Å

62345

9khk

EMDB-62345, PDB-9khk:
Cryo-EM structure of homomeric TRPC channel, class 2
Method: EM (single particle) / Resolution: 2.9 Å

63533

9lzy

EMDB-63533, PDB-9lzy:
Cryo-EM structure of homomeric TRPC channel with agonists, class 1
Method: EM (single particle) / Resolution: 2.43 Å

63534

9lzz

EMDB-63534, PDB-9lzz:
Cryo-EM structure of homomeric TRPC channel with agonists, class 2
Method: EM (single particle) / Resolution: 3.03 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-YZY:
(2S)-2-(hexadecanoyloxy)-3-hydroxypropyl (9Z)-octadec-9-enoate

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-ZN:
Unknown entry

ChemComp-PTY:
PHOSPHATIDYLETHANOLAMINE / phospholipid*YM

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

PDB-1l55:
ANALYSIS OF THE INTERACTION BETWEEN CHARGED SIDE CHAINS AND THE ALPHA-HELIX DIPOLE USING DESIGNED THERMOSTABLE MUTANTS OF PHAGE T4 LYSOZYME

ChemComp-657:
6-(trifluoromethoxy)-1,3-benzothiazol-2-amine

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / TRP

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