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TitleMechanism of (-)-Englerin A and calcium binding on the human TRPC5 channel.
Journal, issue, pagesProtein Sci, Vol. 34, Issue 8, Page e70218, Year 2025
Publish dateAug 15, 2025
AuthorsYikun Chen / Kangcheng Song / Wenjun Guo / Miao Wei / Lei Chen /
PubMed AbstractThe natural product (-)-Englerin A (EA) selectively inhibits renal cancer cell growth by potently activating TRPC4 and TRPC5-containing ion channels. However, its binding site on these channels has ...The natural product (-)-Englerin A (EA) selectively inhibits renal cancer cell growth by potently activating TRPC4 and TRPC5-containing ion channels. However, its binding site on these channels has remained elusive. In this study, we present two cryo-EM structures of human TRPC5 in complex with EA at 2.5 and 2.6 Å resolution, which reveal the EA-binding site and identify two major conformations influenced by calcium. EA binds between the pore helix and S5/S6 helices of hTRPC5, forming critical hydrophobic and polar interactions that underscore its specificity. Calcium binding at the intracellular domain of TRPC5 induces structural changes that stabilize the domain in a compact conformation. These findings expand our understanding of the structural pharmacology of TRPC5 and provide a framework for investigating calcium regulation in TRPC channels.
External linksProtein Sci / PubMed:40671342 / PubMed Central
MethodsEM (single particle)
Resolution2.48 - 2.62 Å
Structure data

63600

9m36

EMDB-63600, PDB-9m36:
Structure of human TRPC5 in the low Ca environment.
Method: EM (single particle) / Resolution: 2.48 Å

63631

9m4w

EMDB-63631, PDB-9m4w:
Structure of human TRPC5 bound with (-)-englerin A, class 2.
Method: EM (single particle) / Resolution: 2.62 Å

63651

9m5v

EMDB-63651, PDB-9m5v:
Structure of human TRPC5 bound with (-)-englerin A,class1
Method: EM (single particle) / Resolution: 2.53 Å

Chemicals

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

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

PDB-1l5i:
30-CONFORMER NMR ENSEMBLE OF THE N-TERMINAL, DNA-BINDING DOMAIN OF THE REPLICATION INITIATION PROTEIN FROM A GEMINIVIRUS (TOMATO YELLOW LEAF CURL VIRUS-SARDINIA)

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

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / Ion channel / TRPC5 / calcium / (-)-englerin A / cryo-EM

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