2HYQ

Crystal structure of a complex of griffithsin with 6alpha-mannobiose

Summary for 2HYQ

• Entry DOI: 10.2210/pdb2hyq/pdb
• Related: 2GTY 2GUC 2GUD 2GUE 2GUX 2HYR
• Related PRD ID: PRD_900118
• Descriptor: Griffithsin, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose, SULFATE ION, ... (4 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: 27795.65

Authors

Ziolkowska, N.E.,Wlodawer, A. (deposition date: 2006-08-07, release date: 2007-04-24, Last modification date: 2024-11-20)

Primary citation

Ziolkowska, N.E.,Shenoy, S.R.,O'keefe, B.R.,McMahon, J.B.,Palmer, K.E.,Dwek, R.A.,Wormald, M.R.,Wlodawer, A.
Crystallographic, thermodynamic, and molecular modeling studies of the mode of binding of oligosaccharides to the potent antiviral protein griffithsin.
Proteins, 67:661-670, 2007

PubMed Abstract: The mode of binding of oligosaccharides to griffithsin, an antiviral lectin from the red alga Griffithsia sp., was investigated by a combination of X-ray crystallography, isothermal titration calorimetry, and molecular modeling. The structures of complexes of griffithsin with 1-->6alpha-mannobiose and with maltose were solved and refined at the resolution of 2.0 and 1.5 A, respectively. The thermodynamic parameters of binding of 1-->6alpha-mannobiose, maltose, and mannose to griffithsin were determined. Binding profiles of 1-->6alpha-mannobiose and mannose were similar with Kd values of 83.3 microM and 102 microM, respectively. The binding of maltose to griffithsin was significantly weaker, with a fourfold lower affinity (Kd = 394 microM). In all cases the binding at 30 degrees C was entropically rather than enthalpically driven. On the basis of the experimental crystal structures, as well as on previously determined structures of complexes with monosaccharides, it was possible to create a model of a tridentate complex of griffithsin with Man9GlcNAc2, a high mannose oligosaccharide commonly found on the surface of viral glycoproteins. All shorter oligomannoses could be modeled only as bidentate or monodentate complexes with griffithsin. The ability to mediate tight multivalent and multisite interactions with high-mannose oligosaccharides helps to explain the potent antiviral activity of griffithsin.

PubMed: 17340634
DOI: 10.1002/prot.21336

Experimental method

X-RAY DIFFRACTION (2 Å)