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-α-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.
- MeSH
- krystalografie rentgenová MeSH
- lektiny chemie genetika metabolismus MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- mutageneze MeSH
- počítačová simulace MeSH
- Ralstonia solanacearum chemie genetika metabolismus MeSH
- receptory buněčného povrchu chemie MeSH
- sacharidové sekvence MeSH
- software MeSH
- vazebná místa MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
1. vyd. 268 s. : il. ; 20 cm
- Klíčová slova
- ájurvéda,
- MeSH
- komplementární terapie metody MeSH
- nádory prevence a kontrola terapie MeSH
- Publikační typ
- populární práce MeSH
- příručky MeSH
