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10.1074/jbc.M115.701425 http://scihub22266oqcxt.onion/10.1074/jbc.M115.701425 C4817157!4817157!26833566     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       J+Biol+Chem 2016 ; 291 (14): 7230-40 Nephropedia Template TP {{tp|p=26833566|t=2016. Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin*? |pdf=|usr=}}{{26833566}} gab.com Text Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin* JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26833566 #FOAvip Streptococcus sanguinis is a leading cause of infective endocarditis, a life-threatening infection of the cardiovascular system. An important interaction in the pathogenesis of infective endocarditis is attachment of the organisms to host platelets. S. sanguinis expresses a serine-rich repeat adhesin, SrpA, similar in sequence to platelet-binding adhesins associated with increased virulence in this disease. In this study, we determined the first crystal structure of the putative binding region of SrpA (SrpABR) both unliganded and in complex with a synthetic disaccharide ligand at 1.8 and 2.0 ? resolution, respectively. We identified a conserved Thr-Arg motif that orients the sialic acid moiety and is required for binding to platelet monolayers. Furthermore, we propose that sequence insertions in closely related family members contribute to the modulation of structural and functional properties, including the quaternary structure, the tertiary structure, and the ligand-binding site. Twit Text FOAVip Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin* ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=26833566 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26833566 #FOAvip English Wikipedia <ref>{{Cite pmid|26833566}}</ref> Structural Basis for Sialoglycan Binding by the Streptococcus sanguinis SrpA Adhesin*? #MMPMID26833566 Bensing BA; Loukachevitch LV; McCulloch KM; Yu H; Vann KR; Wawrzak Z; Anderson S; Chen X; Sullam PM; Iverson TM J Biol Chem 2016[Apr]; 291 (14): 7230-40 PMID26833566show ga Streptococcus sanguinis is a leading cause of infective endocarditis, a life-threatening infection of the cardiovascular system. An important interaction in the pathogenesis of infective endocarditis is attachment of the organisms to host platelets. S. sanguinis expresses a serine-rich repeat adhesin, SrpA, similar in sequence to platelet-binding adhesins associated with increased virulence in this disease. In this study, we determined the first crystal structure of the putative binding region of SrpA (SrpABR) both unliganded and in complex with a synthetic disaccharide ligand at 1.8 and 2.0 ? resolution, respectively. We identified a conserved Thr-Arg motif that orients the sialic acid moiety and is required for binding to platelet monolayers. Furthermore, we propose that sequence insertions in closely related family members contribute to the modulation of structural and functional properties, including the quaternary structure, the tertiary structure, and the ligand-binding site. äStructural Basis for Sialoglycan Binding by the Streptococcus sanguini(epmc).pdf DeepDyve Pubget Overpricing