2HYR

Crystal structure of a complex of griffithsin with maltose

2HYR の概要

• エントリーDOI: 10.2210/pdb2hyr/pdb
• 関連するPDBエントリー: 2GTY 2GUC 2GUD 2GUE 2GUX 2HYQ
• 関連するBIRD辞書のPRD_ID: PRD_900018
• 分子名称: Griffithsin, alpha-D-glucopyranose-(1-4)-beta-D-glucopyranose, SULFATE ION, ... (6 entities in total)
• 機能のキーワード: griffithsin, lectins, domain swapping, mannose binding, hiv, sars, sugar binding protein
• 由来する生物種: Griffithsia
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28030.47

構造登録者

Ziolkowska, N.E.,Wlodawer, A. (登録日: 2006-08-07, 公開日: 2007-04-24, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.51 Å)