| http://purl.uniprot.org/citations/17696333 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17696333 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17696333 | http://www.w3.org/2000/01/rdf-schema#comment | "Spores of Bacillus anthracis are the infectious agent of anthrax. Current antibiotic treatments are limited due to resistance and patient age restrictions; thus, additional targets for therapeutic intervention are needed. One possible candidate is dihydrofolate reductase (DHFR), a biosynthetic enzyme necessary for anthrax pathogenicity. We determined the crystal structure of DHFR from B. anthracis (baDHFR) in complex with methotrexate (MTX; 1) at 2.4 Angstrom resolution. The structure reveals the crucial interactions required for MTX binding and a putative molecular basis for how baDHFR has natural resistance to trimethoprim (TMP; 2). The structure also allows insights for designing selective baDHFR inhibitors that will have weak affinities for the human enzyme. Additionally, we have found that 5-nitro-6-methylamino-isocytosine (MANIC; 3), which inhibits another B. anthracis folate synthesis enzyme, dihydropteroate synthase (DHPS), can also inhibit baDHFR. This provides a starting point for designing multi-target inhibitors that are less likely to induce drug resistance."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.org/dc/terms/identifier | "doi:10.1021/jm070319v"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.org/dc/terms/identifier | "doi:10.1021/jm070319v"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Lee R.E."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Lee R.E."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Dealwis C.G."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Dealwis C.G."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Bennett B.C."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Bennett B.C."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Simmerman R.F."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/author | "Simmerman R.F."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/name | "J. Med. Chem."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/name | "J Med Chem"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/pages | "4374-4381"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/pages | "4374-4381"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/title | "Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/title | "Crystal structure of the anthrax drug target, Bacillus anthracis dihydrofolate reductase."xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/volume | "50"xsd:string |
| http://purl.uniprot.org/citations/17696333 | http://purl.uniprot.org/core/volume | "50"xsd:string |