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10.1038/s41598-017-04120-x http://scihub22266oqcxt.onion/10.1038/s41598-017-04120-x C5479863!5479863!28638151     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Sci+Rep 2017 ; 7 (ä): ä Nephropedia Template TP {{tp|p=28638151|t=2017. The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome |pdf=|usr=}}{{28638151}} gab.com Text The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28638151 #FOAvip Kohlschutter-Tönz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across metazoans, and mutations in Rogdi are linked to KTS. However, how certain mutations in Rogdi abolish its physiological functions and cause KTS is not known. In this study, we determined the crystal structure of human Rogdi protein at atomic resolution. Rogdi forms a novel elongated curved structure comprising the ? domain, a leucine-zipper-like four-helix bundle, and a characteristic ?-sheet domain. Within the ? domain, the N-terminal H1 helix (residues 19?45) pairs with the C-terminal H6 helix (residues 252?287) in an antiparallel manner, indicating that the integrity of the four-helix bundle requires both N- and C-terminal residues. The crystal structure, in conjunction with biochemical data, indicates that the ? domain might undergo a conformational change and provide a structural platform for protein?protein interactions. Disruption of the four-helix bundle by mutation results in significant destabilization of the structure. This study provides structural insights into how certain mutations in Rogdi affect its structure and cause KTS, which has important implications for the development of pharmaceutical agents against this debilitating neurological disease. Twit Text FOAVip The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=28638151 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=28638151 #FOAvip English Wikipedia <ref>{{Cite pmid|28638151}}</ref> The crystal structure of human Rogdi provides insight into the causes of Kohlschutter-Tönz Syndrome #MMPMID28638151 Lee H; Jeong H; Choe J; Jun Y; Lim C; Lee C Sci Rep 2017[]; 7 (ä): ä PMID28638151show ga Kohlschutter-Tönz syndrome (KTS) is a rare autosomal-recessive disorder of childhood onset characterized by global developmental delay, spasticity, epilepsy, and amelogenesis imperfecta. Rogdi, an essential protein, is highly conserved across metazoans, and mutations in Rogdi are linked to KTS. However, how certain mutations in Rogdi abolish its physiological functions and cause KTS is not known. In this study, we determined the crystal structure of human Rogdi protein at atomic resolution. Rogdi forms a novel elongated curved structure comprising the ? domain, a leucine-zipper-like four-helix bundle, and a characteristic ?-sheet domain. Within the ? domain, the N-terminal H1 helix (residues 19?45) pairs with the C-terminal H6 helix (residues 252?287) in an antiparallel manner, indicating that the integrity of the four-helix bundle requires both N- and C-terminal residues. The crystal structure, in conjunction with biochemical data, indicates that the ? domain might undergo a conformational change and provide a structural platform for protein?protein interactions. Disruption of the four-helix bundle by mutation results in significant destabilization of the structure. This study provides structural insights into how certain mutations in Rogdi affect its structure and cause KTS, which has important implications for the development of pharmaceutical agents against this debilitating neurological disease. äThe crystal structure of human Rogdi provides insight into the causes (epmc).pdf DeepDyve Pubget Overpricing