1DYR
THE STRUCTURE OF PNEUMOCYSTIS CARINII DIHYDROFOLATE REDUCTASE TO 1.9 ANGSTROMS RESOLUTION
1DYR の概要
| エントリーDOI | 10.2210/pdb1dyr/pdb |
| 分子名称 | DIHYDROFOLATE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, TRIMETHOPRIM, ... (4 entities in total) |
| 機能のキーワード | oxido-reductase, oxidoreductase |
| 由来する生物種 | Pneumocystis carinii |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 24954.28 |
| 構造登録者 | Champness, J.N.,Achari, A.,Ballantine, S.P.,Bryant, P.K.,Delves, C.J.,Stammers, D.K. (登録日: 1994-09-14, 公開日: 1995-10-15, 最終更新日: 2024-02-07) |
| 主引用文献 | Champness, J.N.,Achari, A.,Ballantine, S.P.,Bryant, P.K.,Delves, C.J.,Stammers, D.K. The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution. Structure, 2:915-924, 1994 Cited by PubMed Abstract: 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. PubMed: 7866743DOI: 10.1016/S0969-2126(94)00093-X 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.86 Å) |
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