Publication details

In Silico Mutagenesis and Docking Study of Ralstonia solanacearum RSL Lectin: Performance of Docking Software To Predict Saccharide Binding

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MISHRA Sushil Kumar ADAM Jan WIMMEROVÁ Michaela KOČA Jaroslav

Year of publication 2012
Type Article in Periodical
Magazine / Source Journal of Chemical Information and Modeling
MU Faculty or unit

Central European Institute of Technology

Field Biochemistry
Keywords docking;in silicomutagenesis; lectin; interactions; energy calculations
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Description In this study, in silico mutagenesis and docking in Ralstonia solanacearum lectin (RSL) were carried out, and the ability of several docking software programs to calculate binding affinity was evaluated. In silico mutation of six amino acid residues (Agr17, Glu28, Gly39, Ala40, Trp76, and Trp81) was done, and a total of 114 in silico mutants of RSL were docked with Me-a-l-fucoside. Our results show that polar residues Arg17 and Glu28, as well as nonpolar amino acids Trp76 and Trp81, are crucial for binding. Gly39 may also influence ligand binding because any mutations at this position lead to a change in the binding pocket shape. The Ala40 residue was found to be the most interesting residue for mutagenesis and can affect the selectivity and/or affinity. In general, the docking software used performs better for high affinity binders and fails to place the binding affinities in the correct order.
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