Unusual structural stability and ligand induced alterations in oligomerization of a galectin.
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.
Surolia
A
A
Molecular Biophysics Unit, Indian Institute of Science, Bangalore. surolia@mbu.iisc.ernet.in
Swaminathan
C P
CP
Ramkumar
R
R
Podder
S K
SK
D000818:Animals; D002152:Calorimetry, Differential Scanning; D004355:Drug Stability; D037483:Galectin 1; D037161:Galectins; D006388:Hemagglutinins / Q000737:chemistry* / Q000378:metabolism; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008024:Ligands; D011108:Polymers / Q000737:chemistry / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D012756:Sheep; D013696:Temperature; D013816:Thermodynamics
D037483:Galectin 1; D037161:Galectins; D006388:Hemagglutinins; D037102:Lectins; D008024:Ligands; D011108:Polymers