2NU5

Crystal structure of a complex of griffithsin cocrystallized with N-acetylglucosamine

Summary for 2NU5

• Entry DOI: 10.2210/pdb2nu5/pdb
• Related: 2GTY 2GUC 2GUD 2GUE 2GUX 2HYR 2NUO
• Descriptor: griffithsin, 2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (4 entities in total)
• Functional Keywords: griffithsin; lectins; domain swapping; mannose binding; hiv; sars, antiviral protein, sugar binding protein
• Biological source: Griffithsia sp.
• Total number of polymer chains: 2
• Total formula weight: 27069.12

Authors

Ziolkowska, N.E.,Wlodawer, A. (deposition date: 2006-11-08, 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

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: 17567736
DOI: 10.1110/ps.072889407

Experimental method

X-RAY DIFFRACTION (1.564 Å)