Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine. Export

@article{citeulike:3180053, abstract = {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.}, address = {Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, MD 21702-1201, USA.}, author = {Zi\'{o}{\l}kowska, N. E. and Shenoy, S. R. and O'Keefe, B. R. and Wlodawer, A.}, citeulike-article-id = {3180053}, citeulike-linkout-0 = {http://dx.doi.org/10.1110/ps.072889407}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/17567736}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=17567736}, doi = {10.1110/ps.072889407}, issn = {0961-8368}, journal = {Protein science : a publication of the Protein Society}, keywords = {benthamiana, griffithsin, lectin, tmv}, month = {July}, number = {7}, pages = {1485--1489}, posted-at = {2008-09-01 22:43:56}, priority = {0}, title = {Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine.}, url = {http://dx.doi.org/10.1110/ps.072889407}, volume = {16}, year = {2007} }

TY - JOUR ID - citeulike:3180053 L3 - citeulike-article-id:3180053 N2 - 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. IS - 7 JF - Protein science : a publication of the Protein Society SN - 0961-8368 AD - Protein Structure Section, Macromolecular Crystallography Laboratory, National Cancer Institute, NCI-Frederick, MD 21702-1201, USA. EP - 1489 TI - Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine. VL - 16 SP - 1485 KW - benthamiana KW - griffithsin KW - lectin KW - tmv AU - Ziółkowska, NE AU - Shenoy, SR AU - O'Keefe, BR AU - Wlodawer, A PY - 2007/07// UR - http://dx.doi.org/10.1110/ps.072889407 ER -