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, DOI https://doi.org/10.1007/s00894-002-0115-8.
Full text not available from this repository.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 |
|---|---|
| Funders: | UNSPECIFIED |
| 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 |
Actions (login required)
 |
View Item |
