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Biophysical Feature, Crystallization and X-ray Crystallographic Studies of Toxascaris leonina Galectin

  • Sung, Min-Kyung (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jeong, Mi-Suk (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Lee, Woo-Chul (Division of Magnetic Resonance, Korea Basic Science Institute) ;
  • Song, Jeong-Hyun (Division of Magnetic Resonance, Korea Basic Science Institute) ;
  • Kim, Hye-Yeon (Division of Magnetic Resonance, Korea Basic Science Institute) ;
  • Cho, Min-Kyoung (Department of Parasitology, School of Medicine, Pusan National University) ;
  • Yu, Hak-Sun (Department of Parasitology, School of Medicine, Pusan National University) ;
  • Jang, Se-Bok (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • Received : 2011.09.26
  • Accepted : 2011.11.21
  • Published : 2012.01.20

Abstract

Galectins are generally believed to be potential candidates for use in the development of novel antiinflammatory agents or as selective modulators of the immune response. In particular, galectin-9 exhibits some of the extracellular functions, including cell aggregation, adhesion, chemoattraction, activation, and apoptosis. Tl-galectin (Tl-gal, galectin-9 homologue gene) was isolated from an adult worm of the Toxascaris leonina. The full-length Tl-gal gene, which was incorporated into pET-28a, was overexpressed in E. coli and purified by nickel affinity and gel filtration chromatographies. The purified Tl-gal was crystallized using the hangingdrop vapor-diffusion method. The crystal belonged to the tetragonal space group $P4_1$, with unit-cell parameters of a = b = $75.7\AA$ and c = $248.4\AA$. The crystals were obtained at $20^{\circ}C$ and diffracted to a resolution of $3.0\AA$. The asymmetric unit contained four molecules of Tl-gal, which gave a crystal volume per protein mass (Vm) of $2.8\AA^3Da^{-1}$ and a solvent content of 54.1%.

Keywords

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