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10.1073/pnas.1810719115 http://scihub22266oqcxt.onion/10.1073/pnas.1810719115 30108148!6126765!30108148     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Proc+Natl+Acad+Sci+U+S+A 2018 ; 115 (35): E8201-E8210 Nephropedia Template TP {{tp|p=30108148|t=2018. Structure of the mammalian TRPM7, a magnesium channel required during embryonic development |pdf=|usr=}}{{30108148}} gab.com Text Structure of the mammalian TRPM7, a magnesium channel required during embryonic development JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=30108148 #FOAvip The transient receptor potential ion channel subfamily M, member 7 (TRPM7), is a ubiquitously expressed protein that is required for mouse embryonic development. TRPM7 contains both an ion channel and an alpha-kinase. The channel domain comprises a nonselective cation channel with notable permeability to Mg(2+) and Zn(2+) Here, we report the closed state structures of the mouse TRPM7 channel domain in three different ionic conditions to overall resolutions of 3.3, 3.7, and 4.1 A. The structures reveal key residues for an ion binding site in the selectivity filter, with proposed partially hydrated Mg(2+) ions occupying the center of the conduction pore. In high [Mg(2+)], a prominent external disulfide bond is found in the pore helix, which is essential for ion channel function. Our results provide a structural framework for understanding the TRPM1/3/6/7 subfamily and extend the knowledge base upon which to study the diversity and evolution of TRP channels. Twit Text FOAVip Structure of the mammalian TRPM7, a magnesium channel required during embryonic development ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=30108148 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=30108148 #FOAvip English Wikipedia <ref>{{Cite pmid|30108148}}</ref> Structure of the mammalian TRPM7, a magnesium channel required during embryonic development #MMPMID30108148 Duan J; Li Z; Li J; Hulse RE; Santa-Cruz A; Valinsky WC; Abiria SA; Krapivinsky G; Zhang J; Clapham DE Proc Natl Acad Sci U S A 2018[Aug]; 115 (35): E8201-E8210 PMID30108148show ga The transient receptor potential ion channel subfamily M, member 7 (TRPM7), is a ubiquitously expressed protein that is required for mouse embryonic development. TRPM7 contains both an ion channel and an alpha-kinase. The channel domain comprises a nonselective cation channel with notable permeability to Mg(2+) and Zn(2+) Here, we report the closed state structures of the mouse TRPM7 channel domain in three different ionic conditions to overall resolutions of 3.3, 3.7, and 4.1 A. The structures reveal key residues for an ion binding site in the selectivity filter, with proposed partially hydrated Mg(2+) ions occupying the center of the conduction pore. In high [Mg(2+)], a prominent external disulfide bond is found in the pore helix, which is essential for ion channel function. Our results provide a structural framework for understanding the TRPM1/3/6/7 subfamily and extend the knowledge base upon which to study the diversity and evolution of TRP channels. |*Embryo, Mammalian[MESH] |*Embryonic Development[MESH] |*Evolution, Molecular[MESH] |Animals[MESH] |Mice[MESH] |Protein Domains[MESH]Structure of the mammalian TRPM7, a magnesium channel required during (epmc).pdf DeepDyve Pubget Overpricing