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Structure paper

TitleStructure of the human TRPM4 ion channel in a lipid nanodisc.
Journal, issue, pagesScience, Vol. 359, Issue 6372, Page 228-232, Year 2018
Publish dateJan 12, 2018
AuthorsHenriette E Autzen / Alexander G Myasnikov / Melody G Campbell / Daniel Asarnow / David Julius / Yifan Cheng /
PubMed AbstractTransient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular ...Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo-electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening.
External linksScience / PubMed:29217581 / PubMed Central
MethodsEM (single particle)
Resolution3.1 - 3.2 Å
Structure data

7132

6bqr

EMDB-7132, PDB-6bqr:
Human TRPM4 ion channel in lipid nanodiscs in a calcium-free state
Method: EM (single particle) / Resolution: 3.2 Å

7133

6bqv

EMDB-7133, PDB-6bqv:
Human TRPM4 ion channel in lipid nanodiscs in a calcium-bound state
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-CA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / TRPM4 / TRPM channel / TRP channel

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