The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution.

Journal article

BACKGROUND: The fungal pathogen Pneumocystis carinii causes a pneumonia which is an opportunistic infection of AIDS patients. Current therapy includes the dihydrofolate reductase (DHFR) inhibitor trimethoprim which is selective but only a relatively weak inhibitor of the enzyme for P. carinii. Determination of the three-dimensional structure of the enzyme should form the basis for design of more potent and selective therapeutic agents for treatment of the disease. RESULTS: The structure of P....

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Authors: Champness, J; Achari, A; Ballantine, S; Bryant, P; Delves, C

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 2
• Issue: 10
• Pages: 915-924
• Publication date: 1994-10-01
• DOI: 10.1016/s0969-2126(94)00093-x
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Humans; Protein Folding; Amino Acid Sequence; Sequence Homology, Amino Acid; Escherichia coli; Folic Acid Antagonists; Tetrahydrofolate Dehydrogenase; Trimethoprim; Mice; Leukemia L1210; NADP; Binding Sites; Pneumocystis; Models, Molecular; Protein Conformation; Ligands; Molecular Structure; Molecular Sequence Data; Animals