Unusual structural stability and ligand induced alterations in oligomerization of a galectin

FEBS Letters

Surolia, Avadhesha¹  Podder, Sunil K²  Ramkumar, Radha²  Swaminathan, Chittoor P¹ 

[1]Molecular Biophysics Unit, Indian Institute of Science, Bangalore-560 012, India

[2]Department of Biochemistry, Indian Institute of Science, Bangalore-560 012, India

关键词: S-type lectin;    Oligomerization;    Differential Scanning Calorimetry;    DSC;    differential scanning calorimetry;    ITC;    isothermal titration calorimetry;    L-14;    14-kDa S-type lectin;   

DOI  :  10.1016/S0014-5793(97)00432-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Abstract L-14, a 14-kDa S-type lectin shows the jelly roll tertiary structural fold akin to legume lectins yet, unlike them, it does not dissociate on thermal unfolding. In the absence of ligand L-14 displays denaturation transitions corresponding to tetrameric and octameric entities. The presence of complementary ligand reduces the association of L-14, which is in stark contrast with legume lectins where no alterations in quaternary structures are brought about by saccharides. From the magnitude of the increase in denaturation temperature induced by disaccharides the binding constants calculated from differential scanning calorimetry are comparable with those extrapolated from titration calorimetry indicating that L-14 interacts with ligands essentially in the folded state.

【 授权许可】

Unknown