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10.1016/j.cell.2013.04.049 http://scihub22266oqcxt.onion/10.1016/j.cell.2013.04.049 C4007204!4007204!23746848     free     free     free       Cell 2013 ; 153 (6): 1379-93 Nephropedia Template TP {{tp|p=23746848|t=2013. Reshaping Antibody Diversity |pdf=|usr=}}{{23746848}} gab.com Text Reshaping Antibody Diversity JO: Cell http://www.kidney.de/pget.php?&tw=1&pmid=23746848 #FOAvip Unlike humans or mice, some species have limited genome encoded combinatorial diversity potential, yet mount a robust antibody response. Cows are unusual in having exceptionally long CDR H3 loops and few V-regions, but the mechanism for creating diversity is not understood. Deep sequencing revealed that ultralong CDR H3s contain a remarkable complexity of cysteines, suggesting that disulfide-bonded mini-domains may arise during repertoire development. Indeed, crystal structures of two cow antibodies reveal that these CDR H3s form a very unusual architecture composed of a ?-strand ?stalk? that supports a structurally diverse, disulfide-bonded, ?knob? domain. Sequence analysis suggests that diversity arises from somatic hypermutation of an ultralong DH with a severe codon bias towards mutation to cysteine. These unusual antibodies can be elicited to recognize defined antigens through the knob domain. Thus, the bovine immune system produces an antibody repertoire composed of CDR H3s of unprecedented length that fold into a diversity of mini-domains generated through combinations of somatically generated disulfides. Twit Text FOAVip Reshaping Antibody Diversity ????Cell http://www.kidney.de/pget.php?&tw=1&pmid=23746848 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23746848 #FOAvip English Wikipedia <ref>{{Cite pmid|23746848}}</ref> Reshaping Antibody Diversity #MMPMID23746848 Wang F; Ekiert DC; Ahmad I; Yu W; Zhang Y; Bazirgan O; Torkamani A; Raudsepp T; Mwangi W; Criscitiello MF; Wilson IA; Schultz PG; Smider VV Cell 2013[Jun]; 153 (6): 1379-93 PMID23746848show ga Unlike humans or mice, some species have limited genome encoded combinatorial diversity potential, yet mount a robust antibody response. Cows are unusual in having exceptionally long CDR H3 loops and few V-regions, but the mechanism for creating diversity is not understood. Deep sequencing revealed that ultralong CDR H3s contain a remarkable complexity of cysteines, suggesting that disulfide-bonded mini-domains may arise during repertoire development. Indeed, crystal structures of two cow antibodies reveal that these CDR H3s form a very unusual architecture composed of a ?-strand ?stalk? that supports a structurally diverse, disulfide-bonded, ?knob? domain. Sequence analysis suggests that diversity arises from somatic hypermutation of an ultralong DH with a severe codon bias towards mutation to cysteine. These unusual antibodies can be elicited to recognize defined antigens through the knob domain. Thus, the bovine immune system produces an antibody repertoire composed of CDR H3s of unprecedented length that fold into a diversity of mini-domains generated through combinations of somatically generated disulfides. äReshaping Antibody Diversity (epmc).pdf DeepDyve Pubget Overpricing