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

Bulletin of the Korean chemical society

Jeong Hyun Song¹  Min Kyoung Cho¹  Minkyung Sung¹  Mi Suk Jeong¹  Hye Yeon Kim¹  Se Bok Jang¹  Hak Sun Yu¹  Woo Chul Lee¹ 

关键词: Crystallization;    X-ray analysis;    Toxascaris leonina;    Galectin;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

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 P41, with unit-cell parameters of a = b = 75.7 Å and c = 248.4 Å. The crystals were obtained at 20 oC and diffracted to a resolution of 3.0 Å. The asymmetric unit contained four molecules of Tl-gal, which gave a crystal volume per protein mass (Vm) of 2.8 Å3 Da−1 and a solvent content of 54.1%.

【 授权许可】

Unknown