A Comparison of the Conformations of the 5′-Triphosphates of Zidovudine (AZT) and Thymidine Bound to HIV-1 Reverse Transcriptase
| Autor: | C. W. Andrews, A. E. Aulabaugh, G.R. Painter |
|---|---|
| Rok vydání: | 1993 |
| Předmět: |
Magnetic Resonance Spectroscopy
Stereochemistry Biophysics Human immunodeficiency virus (HIV) Nuclear Overhauser effect Biology medicine.disease_cause Biochemistry Zidovudine chemistry.chemical_compound medicine Molecular Biology chemistry.chemical_classification Molecular Structure RNA-Directed DNA Polymerase Glycosidic bond Cell Biology HIV Reverse Transcriptase Recombinant Proteins In vitro Reverse transcriptase Enzyme chemistry HIV-1 Thymidine Protein Binding medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 191:1166-1171 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1993.1339 |
| Popis: | Nuclear Overhauser effect experiments were performed at 500 MHz to determine the conformations of AZTTP and dTTP when bound to HIV-1 reverse transcriptase. The conformations of both ligands were found to be similar in the bound state. The orientation of the glycosidic angle is anti (chi = -120 degrees +/- 12 for AZTTP and -110 degrees +/- 12 for dTTP), gamma is +sc and the pucker of the 3'-azido-2',3'-dideoxy- and 2'-deoxyribose rings is predominantly C4' exo (P = 60 degrees +/- 10 for AZTTP and 55 degrees +/- 8 for dTTP). These results indicate that the unusual C4'endo/C3'exo pucker (P = 215 degrees) reported for the dideoxyribose ring of AZT in the solid state does not play a role in the interaction of HIV-1 reverse transcriptase with AZTTP. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|