The structure of mouse L1210 dihydrofolate reductase-drug complexes and the construction of a model of human enzyme.

Journal article

The structure of mouse L1210 dihydrofolate reductase (DHFR) complexed with NADPH and trimethoprim has been refined at 2.0 A resolution. The analogous complex with NADPH and methotrexate has been refined at 2.5 A resolution. These structures reveal for the first time details of drug interactions with a mammalian DHFR, which are compared with those observed from previous X-ray investigations of DHFR/inhibitor complexes. The refined L1210 structure has been used as the basis for the construction...

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Authors: Stammers, D; Champness, J; Beddell, C; Dann, J; Eliopoulos, E

• Publication status: Published
• Journal: FEBS letters
• Volume: 218
• Issue: 1
• Pages: 178-184
• Publication date: 1987-06-01
• DOI: 10.1016/0014-5793(87)81042-6
• EISSN: 1873-3468
• ISSN: 0014-5793
• Language: English
• Keywords: Species Specificity; NADP; Humans; Protein Binding; X-Ray Diffraction; Trimethoprim; Tetrahydrofolate Dehydrogenase; Leukemia L1210; Neoplasm Proteins; Binding Sites; Protein Conformation; Models, Molecular; Mice; Animals