The conformations of trimethoprim/E. coli dihydrofolate reductase complexes A 15N and 31P NMR study

Fu yung Huang, Qing Xian Yang, Tai huang Huang, Leslie Gelbaum, Lee F. Kuyper

研究成果: Article

5 引文 斯高帕斯(Scopus)

摘要

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 complex.

原文English
頁(從 - 到)44-46
頁數3
期刊FEBS Letters
283
發行號1
DOIs
出版狀態Published - 1991 五月 20

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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