| Literature DB >> 3595861 |
D K Stammers, J N Champness, C R Beddell, J G Dann, E Eliopoulos, A J Geddes, D Ogg, A C North.
Abstract
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 of a model of the human enzyme. There are only twenty-one sequence differences between mouse L1210 and human DHFRs, and all but two of these are located close to the molecular surface: a strong indication that the active sites are essentially identical in these two mammalian enzymes.Entities:
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Year: 1987 PMID： 3595861 DOI： 10.1016/0014-5793(87)81042-6
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124