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Title: | Computational docking of L-arginine and its structural analogues to C-terminal domain of Escherichia coli arginine repressor protein (ArgRc) | Authors: | Kueh, R. Rahman, N.A. Merican, A.F. |
Issue Date: | 2003 | Abstract: | The arginine repressor (ArgR) of Escherichia coli binds to six L-arginine molecules that act as its corepressor in order to bind to DNA. The binding of L-arginine molecules as well as its structural analogues is compared by means of computational docking. A gridbased energy evaluation method combined with a Monte Carlo simulated annealing process was used in the automated docking. For all ligands, the docking procedure proposed more than one binding site in the C-terminal domain of ArgR (ArgRc). Interaction patterns of ArgRc with L-arginine were also observed for L-canavanine and L-citrulline. L-Lysine and L-homoarginine, on the other hand, were shown to bind poorly at the binding site. | URI: | http://dspace.uniten.edu.my/jspui/handle/123456789/9835 |
Appears in Collections: | COE Scholarly Publication |
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