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10.1093/nar/gkv909 http://scihub22266oqcxt.onion/10.1093/nar/gkv909 C4605324!4605324!26384426     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26384426.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nucleic+Acids+Res 2015 ; 43 (18): 8615-26 Nephropedia Template TP {{tp|p=26384426|t=2015. Structure of a human translation termination complex |pdf=|usr=}}{{26384426}} gab.com Text Structure of a human translation termination complex JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26384426 #FOAvip In contrast to bacteria that have two release factors, RF1 and RF2, eukaryotes only possess one unrelated release factor eRF1, which recognizes all three stop codons of the mRNA and hydrolyses the peptidyl-tRNA bond. While the molecular basis for bacterial termination has been elucidated, high-resolution structures of eukaryotic termination complexes have been lacking. Here we present a 3.8 Å structure of a human translation termination complex with eRF1 decoding a UAA(A) stop codon. The complex was formed using the human cytomegalovirus (hCMV) stalling peptide, which perturbs the peptidyltransferase center (PTC) to silence the hydrolysis activity of eRF1. Moreover, unlike sense codons or bacterial stop codons, the UAA stop codon adopts a U-turn-like conformation within a pocket formed by eRF1 and the ribosome. Inducing the U-turn conformation for stop codon recognition rationalizes how decoding by eRF1 includes monitoring geometry in order to discriminate against sense codons. Twit Text FOAVip Structure of a human translation termination complex ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=26384426 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26384426 #FOAvip English Wikipedia <ref>{{Cite pmid|26384426}}</ref> Structure of a human translation termination complex #MMPMID26384426 Matheisl S; Berninghausen O; Becker T; Beckmann R Nucleic Acids Res 2015[Oct]; 43 (18): 8615-26 PMID26384426show ga In contrast to bacteria that have two release factors, RF1 and RF2, eukaryotes only possess one unrelated release factor eRF1, which recognizes all three stop codons of the mRNA and hydrolyses the peptidyl-tRNA bond. While the molecular basis for bacterial termination has been elucidated, high-resolution structures of eukaryotic termination complexes have been lacking. Here we present a 3.8 Å structure of a human translation termination complex with eRF1 decoding a UAA(A) stop codon. The complex was formed using the human cytomegalovirus (hCMV) stalling peptide, which perturbs the peptidyltransferase center (PTC) to silence the hydrolysis activity of eRF1. Moreover, unlike sense codons or bacterial stop codons, the UAA stop codon adopts a U-turn-like conformation within a pocket formed by eRF1 and the ribosome. Inducing the U-turn conformation for stop codon recognition rationalizes how decoding by eRF1 includes monitoring geometry in order to discriminate against sense codons. äStructure of a human translation termination complex (epmc).pdf DeepDyve Pubget Overpricing