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TitleStructure of full-length human TRPM4.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 115, Issue 10, Page 2377-2382, Year 2018
Publish dateMar 6, 2018
AuthorsJingjing Duan / Zongli Li / Jian Li / Ana Santa-Cruz / Silvia Sanchez-Martinez / Jin Zhang / David E Clapham /
PubMed AbstractTransient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in ...Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π-π bonds and cation-π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4.
External linksProc Natl Acad Sci U S A / PubMed:29463718 / PubMed Central
MethodsEM (single particle)
Resolution3.7 Å
Structure data

7299

6bwi

EMDB-7299, PDB-6bwi:
3.7 angstrom cryoEM structure of full length human TRPM4
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-NA:
Unknown entry

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • Mus musculus (house mouse)
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / CryoEM / human full length TRPM7

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