2NUO
Crystal structure of a complex of griffithsin with glucose
Summary for 2NUO
| Entry DOI | 10.2210/pdb2nuo/pdb |
| Related | 2gty 2guc 2gud 2gue 2gux 2hyq 2hyr 2i43 |
| Descriptor | Griffithsin, beta-D-glucopyranose, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | griffithsin, lectins, domain swapping, mannose binding, hiv, sars, sugar binding protein |
| Biological source | Griffithsia |
| Total number of polymer chains | 2 |
| Total formula weight | 26692.75 |
| Authors | Ziolkowska, N.E.,Wlodawer, A. (deposition date: 2006-11-09, release date: 2007-08-07, Last modification date: 2024-10-30) |
| Primary citation | Ziolkowska, N.E.,Shenoy, S.R.,O'Keefe, B.R.,Wlodawer, A. Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine. Protein Sci., 16:1485-1489, 2007 Cited by PubMed 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. PubMed: 17567736DOI: 10.1110/ps.072889407 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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