Structural Characterization , Docking and Dynamics Simulations of Canavalia Bonariensis Lectin

Lectins are proteins that bind specifically and reversibly to carbohydrates. These proteins, in particular those from plants, are important tools in glycobiochemistry and glycobiology. Canavalia bonariensis Lindl is a species from the Leguminosae family, Papilionoideae subfamily, Phaseoleae tribe and Diocleinae sub tribe. It contains a glucose/mannose lectin, here in termed as CaBo, previously purified. The primary sequence of the lectin was determined by a combination of tandem mass spectrometry and molecular biology by amplification of the lectin gene isolated from the genomics DNA of the plant. CaBo presented high sequence similarity with lectins from the same sub tribe. From its primary structure, it was possible to predict the tridimensional structure of CaBo by homology with the lectin from Canavalia gladiata. The protein was subjected to ligand screening, both monosaccharides and dimannosides, by molecular docking, and the stability and binding dynamics of CaBo were assessed by molecular dynamics.