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10.1038/s41467-022-30919-y http://scihub22266oqcxt.onion/10.1038/s41467-022-30919-y 35662242!9166780!35662242     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=35662242&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215       Nat+Commun 2022 ; 13 (1): 3113 Nephropedia Template TP {{tp|p=35662242|t=2022. Structures of a mammalian TRPM8 in closed state |pdf=|usr=}}{{35662242}} gab.com Text Structures of a mammalian TRPM8 in closed state JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35662242 #FOAvip Transient receptor potential melastatin 8 (TRPM8) channel is a Ca(2+)-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(2)), and desensitized by Ca(2+). Here we have determined electron cryo-microscopy structures of mouse TRPM8 in the absence of ligand, and in the presence of Ca(2+) and icilin at 2.5-3.2 A 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(2+). Ca(2+) 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. Twit Text FOAVip Structures of a mammalian TRPM8 in closed state ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35662242 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35662242 #FOAvip English Wikipedia <ref>{{Cite pmid|35662242}}</ref> Structures of a mammalian TRPM8 in closed state #MMPMID35662242 Zhao C; Xie Y; Xu L; Ye F; Xu X; Yang W; Yang F; Guo J Nat Commun 2022[Jun]; 13 (1): 3113 PMID35662242show ga Transient receptor potential melastatin 8 (TRPM8) channel is a Ca(2+)-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(2)), and desensitized by Ca(2+). Here we have determined electron cryo-microscopy structures of mouse TRPM8 in the absence of ligand, and in the presence of Ca(2+) and icilin at 2.5-3.2 A 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(2+). Ca(2+) 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. |*TRPM Cation Channels/metabolism[MESH] |*Transient Receptor Potential Channels/metabolism[MESH] |Animals[MESH] |Cold Temperature[MESH] |Ligands[MESH] |Mammals/metabolism[MESH] |Menthol/pharmacology[MESH] |Mice[MESH]Structures of a mammalian TRPM8 in closed state (epmc).pdf DeepDyve Pubget Overpricing