Computational Docking of L-arginine and its structural analogues to C-terminal domain of escherichia coli arginine repressor protein (ARGRC)

Document Type

Article

Publication Date

1-1-2003

Abstract

The arginine repressor (ArgR) of Escherichia coli binds to six L-arginine molecules that act as its co-repressor 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 grid-based 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.

Keywords

Arginine repressor, L-arginine structural analogues, computational, docking, dna-binding domain, automated docking, bacillus-stearothermophilus, operator, site, gene

Publication Title

Journal of Molecular Modeling

ISSN

0948-5023

Divisions

InstituteofBiologicalSciences

Volume

9

Issue

2

Additional Information

Institute of Biological Sciences, Faculty of Science Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA

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