Equine infectious anemia virus Tat is a predominantly helical protein
Open Access
- 1 December 1993
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 218 (3) , 973-976
- https://doi.org/10.1111/j.1432-1033.1993.tb18455.x
Abstract
Nuclear magnetic resonance (NMR) spectroscopy revealed features of the secondary structure of the equine infectious anemia virus (EIAV) Tat protein in solution. We could show that this protein, which is required in the replication cycle of lentiviruses, forms a predominantly helical structure in trifluoroethanol/water (40% by vol.) solution. In particular, the basic RNA‐binding region and the adjacent core domain, which are highly conserved among lentiviral Tat proteins, show helix‐type secondary structure under these conditions. Our observations, in concert with recent biochemical data from other laboratories, suggest that the core sequence region and the basic sequence region form interdependent structural domains, both possibly necessary for correct RNA binding.Keywords
This publication has 30 references indexed in Scilit:
- Sequence-specific resonance assignments of the proton NMR spectra of a synthetic, biologically active EIAV-Tat ProteinBiochemistry, 1993
- Progress in protein structure prediction?Trends in Biochemical Sciences, 1993
- High Affinity Binding of TAR RNA by the Human Immunodeficiency Virus Type-1 tat Protein Requires Base-pairs in the RNA Stem and Amino Acid Residues Flanking the Basic RegionJournal of Molecular Biology, 1993
- Characterization of recombinant HIV-1 Tat and its interaction with TAR RNABiochemistry, 1992
- Effect of trifluoroethanol on protein secondary structure: an NMR and CD study using a synthetic actin peptideBiochemistry, 1992
- The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopyBiochemistry, 1992
- The structure of ColE1 rop in solutionJournal of Biomolecular NMR, 1991
- Predicting the secondary structure of globular proteins using neural network modelsJournal of Molecular Biology, 1988
- Structure of the ColE1 Rop protein at 1.7 Å resolutionJournal of Molecular Biology, 1987
- Conformational parameters for amino acids in helical, β-sheet, and random coil regions calculated from proteinsBiochemistry, 1974