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Multiple ligand-binding modes in bacterial R67 dihydrofolate reductase

Alonso, Hernan; Gillies, Malcolm; Cummins, Peter; Bliznyuk, Andrei; Gready, Jill

Description

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]

CollectionsANU Research Publications
Date published: 2005
Type: Journal article
URI: http://hdl.handle.net/1885/73931
Source: Journal of Computer-Aided Molecular Design
DOI: 10.1007/s10822-005-3693-6

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