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Structure paper

TitleCryo-EM structure of the heteromeric TRPC1/TRPC4 channel.
Journal, issue, pagesNat Struct Mol Biol, Year 2024
Publish dateOct 30, 2024
AuthorsJongdae Won / Jinhyeong Kim / Jinsung Kim / Juyeon Ko / Christine Haewon Park / Byeongseok Jeong / Sang-Eun Lee / Hyeongseop Jeong / Sun-Hong Kim / Hyunwoo Park / Insuk So / Hyung Ho Lee /
PubMed AbstractTransient receptor potential (TRP) ion channels have a crucial role as cellular sensors, mediating diverse physical and chemical stimuli. The formation of heteromeric structures expands the ...Transient receptor potential (TRP) ion channels have a crucial role as cellular sensors, mediating diverse physical and chemical stimuli. The formation of heteromeric structures expands the functionality of TRP channels; however, their molecular architecture remains largely unknown. Here we present the cryo-electron microscopy structures of the human TRPC1/TRPC4 heteromer in the apo and antagonist-bound states, both consisting of one TRPC1 subunit and three TRPC4 subunits. The heteromer structure reveals a distinct ion-conduction pathway, including an asymmetrically constricted selectivity filter and an asymmetric lower gate, primarily attributed to the incorporation of TRPC1. Through a structure-guided electrophysiological assay, we show that both the selectivity filter and the lower part of the S6 helix participate in deciding overall preference for permeating monovalent cations. Moreover, we reveal that the introduction of one lysine residue of TRPC1 into the tetrameric central cavity is enough to render one of the most important functional consequences of TRPC heteromerization: reduced calcium permeability. Our results establish a framework for addressing the structure-function relationship of the heteromeric TRP channels.
External linksNat Struct Mol Biol / PubMed:39478185
MethodsEM (single particle)
Resolution2.82 - 3.43 Å
Structure data

37718

8wpl

EMDB-37718, PDB-8wpl:
Cryo-EM structure of the human TRPC1/C4 heteromer
Method: EM (single particle) / Resolution: 3.04 Å

37719

8wpm

EMDB-37719, PDB-8wpm:
Cryo-EM structure of the human TRPC1/C4 heteromer in complex with Pico145
Method: EM (single particle) / Resolution: 3.43 Å

37720

8wpn

EMDB-37720, PDB-8wpn:
Cryo-EM structure of the human TRPC4 in lipid nanodiscs
Method: EM (single particle) / Resolution: 2.82 Å

Chemicals

ChemComp-LPP:
2-(HEXADECANOYLOXY)-1-[(PHOSPHONOOXY)METHYL]ETHYL HEXADECANOATE / phospholipid*YM

ChemComp-ZN:
Unknown entry

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-CA:
Unknown entry

ChemComp-PJQ:
7-[(4-chlorophenyl)methyl]-3-methyl-1-(3-oxidanylpropyl)-8-[3-(trifluoromethyloxy)phenoxy]purine-2,6-dione

Source
  • homo sapiens (human)
KeywordsMETAL TRANSPORT / transient receptor potential

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