Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine.,Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A Protein Sci. 2007 Jul;16(7):1485-9. Epub 2007 Jun 13. PMID:17567736[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ziolkowska NE, Shenoy SR, O'Keefe BR, Wlodawer A. Crystallographic studies of the complexes of antiviral protein griffithsin with glucose and N-acetylglucosamine. Protein Sci. 2007 Jul;16(7):1485-9. Epub 2007 Jun 13. PMID:17567736 doi:10.1110/ps.072889407
