Multiple ligand-binding modes in bacterial R67 dihydrofolate reductase
Alonso, Hernan; Gillies, Malcolm; Cummins, Peter; Bliznyuk, Andrei; Gready, Jill
R67 dihydrofolate reductase (DHFR), a bacterial plasmid-encoded enzyme associated with resistance to the drug trimethoprim, shows neither sequence nor structural homology with the chromosomal DHFR. It presents a highly symmetrical toroidal structure, where four identical monomers contribute to the unique central active-site pore. Two reactants (dihydrofolate, DHF), two cofactors (NADPH) or one of each (R67•DHF•NADPH) can be found simultaneously within the active site, the last one being the...[Show more]
|Collections||ANU Research Publications|
|Source:||Journal of Computer-Aided Molecular Design|
|01_Alonso_Multiple_ligand-binding_modes_2005.pdf||797.58 kB||Adobe PDF||Request a copy|
Items in Open Research are protected by copyright, with all rights reserved, unless otherwise indicated.
Updated: 17 November 2022/ Responsible Officer: University Librarian/ Page Contact: Library Systems & Web Coordinator