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7WRB

Mouse TRPM8 in LMNG in the presence of calcium

Summary for 7WRB
Entry DOI10.2210/pdb7wrb/pdb
EMDB information32721
DescriptorTransient receptor potential cation channel subfamily M member 8, CALCIUM ION (2 entities in total)
Functional Keywordstrpm8, transport protein
Biological sourceMus musculus (house mouse)
Total number of polymer chains4
Total formula weight518329.22
Authors
Zhao, C.,Xie, Y.,Guo, J. (deposition date: 2022-01-26, release date: 2022-06-22, Last modification date: 2024-10-16)
Primary citationZhao, C.,Xie, Y.,Xu, L.,Ye, F.,Xu, X.,Yang, W.,Yang, F.,Guo, J.
Structures of a mammalian TRPM8 in closed state.
Nat Commun, 13:3113-3113, 2022
Cited by
PubMed Abstract: Transient receptor potential melastatin 8 (TRPM8) channel is a Ca-permeable non-selective cation channel that acts as the primary cold sensor in humans. TRPM8 is also activated by ligands such as menthol, icilin, and phosphatidylinositol 4,5-bisphosphate (PIP), and desensitized by Ca. Here we have determined electron cryo-microscopy structures of mouse TRPM8 in the absence of ligand, and in the presence of Ca and icilin at 2.5-3.2 Å resolution. The ligand-free state TRPM8 structure represents the full-length structure of mammalian TRPM8 channels with a canonical S4-S5 linker and the clearly resolved selectivity filter and outer pore loop. TRPM8 has a short but wide selectivity filter which may account for its permeability to hydrated Ca. Ca and icilin bind in the cytosolic-facing cavity of the voltage-sensing-like domain of TRPM8 but induce little conformational change. All the ligand-bound TRPM8 structures adopt the same closed conformation as the ligand-free structure. This study reveals the overall architecture of mouse TRPM8 and the structural basis for its ligand recognition.
PubMed: 35662242
DOI: 10.1038/s41467-022-30919-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.88 Å)
Structure validation

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