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10.1038/ncomms10356 http://scihub22266oqcxt.onion/10.1038/ncomms10356 C4735555!4735555!26758274     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2016 ; 7 (ä): ä Nephropedia Template TP {{tp|p=26758274|t=2016. Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex |pdf=|usr=}}{{26758274}} gab.com Text Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26758274 #FOAvip The covalent conjugation of a 14-carbon saturated fatty acid (myristic acid) to the amino-terminal glycine residue is critical for some viral proteins to function. This protein lipidation modification, termed N-myristoylation, is targeted by host cytotoxic T lymphocytes (CTLs) that specifically recognize N-myristoylated short peptides; however, the molecular mechanisms underlying lipopeptide antigen (Ag) presentation remain elusive. Here we show that a primate major histocompatibility complex (MHC) class I-encoded protein is capable of binding N-myristoylated 5-mer peptides and presenting them to specific CTLs. A high-resolution X-ray crystallographic analysis of the MHC class I:lipopeptide complex reveals an Ag-binding groove that is elaborately constructed to bind N-myristoylated short peptides rather than prototypic 9-mer peptides. The identification of lipopeptide-specific, MHC class I-restricted CTLs indicates that the widely accepted concept of MHC class I-mediated presentation of long peptides to CTLs may need some modifications to incorporate a novel MHC class I function of lipopeptide Ag presentation. Twit Text FOAVip Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=26758274 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26758274 #FOAvip English Wikipedia <ref>{{Cite pmid|26758274}}</ref> Crystal structure of the N-myristoylated lipopeptide-bound MHC class I complex #MMPMID26758274 Morita D; Yamamoto Y; Mizutani T; Ishikawa T; Suzuki J; Igarashi T; Mori N; Shiina T; Inoko H; Fujita H; Iwai K; Tanaka Y; Mikami B; Sugita M Nat Commun 2016[]; 7 (ä): ä PMID26758274show ga The covalent conjugation of a 14-carbon saturated fatty acid (myristic acid) to the amino-terminal glycine residue is critical for some viral proteins to function. This protein lipidation modification, termed N-myristoylation, is targeted by host cytotoxic T lymphocytes (CTLs) that specifically recognize N-myristoylated short peptides; however, the molecular mechanisms underlying lipopeptide antigen (Ag) presentation remain elusive. Here we show that a primate major histocompatibility complex (MHC) class I-encoded protein is capable of binding N-myristoylated 5-mer peptides and presenting them to specific CTLs. A high-resolution X-ray crystallographic analysis of the MHC class I:lipopeptide complex reveals an Ag-binding groove that is elaborately constructed to bind N-myristoylated short peptides rather than prototypic 9-mer peptides. The identification of lipopeptide-specific, MHC class I-restricted CTLs indicates that the widely accepted concept of MHC class I-mediated presentation of long peptides to CTLs may need some modifications to incorporate a novel MHC class I function of lipopeptide Ag presentation. äCrystal structure of the N-myristoylated lipopeptide-bound MHC class I(epmc).pdf DeepDyve Pubget Overpricing