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10.1110/ps.072889407 http://scihub22266oqcxt.onion/10.1110/ps.072889407 17567736!2206701!17567736     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\17567736.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Protein+Sci 2007 ; 16 (7): 1485-9 Nephropedia Template TP {{tp|p=17567736|t=2007. Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine |pdf=|usr=}}{{17567736}} gab.com Text Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine JO: Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=17567736 #FOAvip Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes. Twit Text FOAVip Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine ????Protein Sci http://www.kidney.de/pget.php?&tw=1&pmid=17567736 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=17567736 #FOAvip English Wikipedia <ref>{{Cite pmid|17567736}}</ref> Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine #MMPMID17567736 Ziolkowska NE; Shenoy SR; O'Keefe BR; Wlodawer A Protein Sci 2007[Jul]; 16 (7): 1485-9 PMID17567736show ga Crystal structures of complexes of an antiviral lectin griffithsin (GRFT) with glucose and N-acetylglucosamine were solved and refined at high resolution. In both complexes, all six monosaccharide-binding sites of GRFT were occupied and the mode of binding was similar to that of mannose. In our previous attempts to obtain a complex with N-acetylglucosamine by soaking, only a single site was occupied; thus, cocrystallization was clearly superior despite lower concentration of the ligand. Isothermal titration calorimetric experiments with N-acetylglucosamine, glucose, and mannose provided enthalpic evidence of distinct binding differences between the three monosaccharides. A comparison of the mode of binding of different monosaccharides is discussed in the context of the antiviral activity of GRFT, based on specific binding to high-mannose-containing complex carbohydrates found on viral envelopes. |Acetylglucosamine/*chemistry/metabolism[MESH] |Antiviral Agents/chemistry/metabolism[MESH] |Crystallography, X-Ray/*methods[MESH] |Glucose/*chemistry/metabolism[MESH] |Lectins/*chemistry/metabolism[MESH] |Mannose/chemistry/metabolism[MESH] |Models, Molecular[MESH]Crystallographic studies of the complexes of antiviral protein griffit(epmc).pdf DeepDyve Pubget Overpricing