| Autor: |
Stockman BJ; Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115., Nirmala NR, Wagner G, Delcamp TJ, DeYarman MT, Freisheim JH |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1991 Jun 03; Vol. 283 (2), pp. 267-9. |
| DOI: |
10.1016/0014-5793(91)80604-2 |
| Abstrakt: |
Dihydrofolate reductase (DHFR) is an intracellular target enzyme for folate antagonist drugs, including methotrexate. In order to compare the binding of methotrexate to human DHFR in solution with that observed in the crystalline state, NMR spectroscopy has been used to determine the conformation of the drug bound to human DHFR in solution. In agreement with what has been observed in the crystalline state, NOE's identified protein and methotrexate protons indicate that methotrexate binds in a non-productive orientation. In contrast to what has been reported for E. coli DHFR in solution, only one bound conformation of methotrexate is observed. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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