02479nas a2200241   4500008004100000022001400041245010300055210006900158260005700227300000800284490000700292520161300299653002101912653001501933653002201948653003301970653002002003100001902023700001802042700002702060700002202087856012802109       2015                        eng d  a1610-294000aIn silico ligand binding studies of cyanogenic beta-glucosidase, dhurrinase-2 from Sorghum bicolor0 aIn silico ligand binding studies of cyanogenic betaglucosidase d  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcJUL  a1840 v213 a<p>Dhurrinase, a cyanogenic beta-glucosidase from Sorghum bicolor is the key enzyme responsible for the hydrolysis of dhurrin to produce toxic hydrogen cyanide, as a part of plant defence mechanism. Dhurrinase 1 (SbDhr1) and dhurrinase 2 (SbDhr2), two isozymes have been isolated and characterized from S. bicolor. However, there is no information in the literature about the three dimensional (3D) structure of SbDhr2 and molecular interactions involved between the protein and ligand. In this study, the three dimensional structure of SbDhr2 was built based on homology modeling by using the X-ray crystallographic structure of its close homologue SbDhr1 as the template. The generated 3D model was energy minimized and the quality was validated by Ramachndran plot, various bioinformatic tools and their relevant parameters. Stability, folding-unfolding and flexibility of the modeled SbDhr2 was evaluated on the basis of RMSD, radius of gyration (R-g) and RMSF values respectively, obtained through molecular dynamic (MD) simulation. Further, molecular docking was performed with its natural substrate dhurrin, one substrate analogue, three un-natural substrates, and one inhibitor. Analysis of molecular interactions in the SbDhr2-ligand complexes revealed the key amino acid residues responsible to stabilize the ligands within the binding pocket through non-bonded interactions and some of them were found to be conserved (Glu239, Tyr381, Trp426, Glu454, Trp511). Reasonably broader substrate specificity of SbDhr2 was explained through the wider entrance passage observed in comparison to SbDhr1.</p>10abeta-Glucosidase10aDhurrinase10aMolecular docking10aMolecular dynamic simulation10aSorghum bicolor1 aMahajan, Chavi1 aPatel, Krunal1 aKhan, Bashir, Mohammad1 aRawal, Shuban, S.  uhttps://library.ncl.res.in/content/silico-ligand-binding-studies-cyanogenic-beta-glucosidase-dhurrinase-2-sorghum-bicolor-1