The conformations of trimethoprim/E. colidihydrofolate reductase complexes A15N and31P NMR study
- 20 May 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 283 (1) , 44-46
- https://doi.org/10.1016/0014-5793(91)80549-i
Abstract
We have employed 15N and 31P NMR techniques to characterize the conformations of trimethoprim (TMP)/E. coli dihydrofolate reductase (DHFR) complexes in the presence and absence of NADPH and NADP+. A single conformation was observed for TMP/DHFR, NADP+/DHFR, NADPH/ DHFR and TMP/NADPH/DHFR complexes. In the ternary complex of TMP/NADP+/DHFR both the 15N and 31P spectra revealed the presence of two conformations. However, the conformations of TMP and NADP+ in the ternary complex may not be correlated, resulting in the possible existence of four conformations for the protein ternary complexKeywords
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