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

Kueh, R. and Rahman, N.A. and Merican, A.F. (2003) Computational Docking of L-arginine and its structural analogues to C-terminal domain of escherichia coli arginine repressor protein (ARGRC). Journal of Molecular Modeling, 9 (2). pp. 88-98. ISSN 0948-5023

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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.

Item Type: Article
Additional Information: Institute of Biological Sciences, Faculty of Science Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA
Uncontrolled Keywords: Arginine repressor, L-arginine structural analogues, computational, docking, dna-binding domain, automated docking, bacillus-stearothermophilus, operator, site, gene
Subjects: Q Science > QH Natural history > QH301 Biology
Divisions: Faculty of Science > Institute of Biological Sciences
Depositing User: Miss Malisa Diana
Date Deposited: 04 Mar 2013 01:43
Last Modified: 04 Mar 2013 01:43
URI: http://eprints.um.edu.my/id/eprint/4944

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