ArticleNucleic acids research2012
Metal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain.Journal of thermal analysis and calorimetry · 2019Article
- A two-nuclease pathway involving RNase H1 is required for primer removal at human mitochondrial OriL.Nucleic acids research · 2018Article
- Identification of drivers for the metamorphic transition of HIV-1 reverse transcriptase.The Biochemical journal · 2017Article
- Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A MgThe journal of physical chemistry. B · 2016Article
- Structural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic Instability.Viruses · 2016Review
- Unfolding the HIV-1 reverse transcriptase RNase H domain--how to lose a molecular tug-of-war.Nucleic acids research · 2016Article
- Article
- Selective unfolding of one Ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation.Nucleic acids research · 2014Article
- Calcium inhibition of ribonuclease H1 two-metal ion catalysis.Journal of the American Chemical Society · 2014Article
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Authors and funding
4 authors.
Funding
Abstract
HIV-1 reverse transcriptase (RT) contains a C-terminal ribonuclease H (RH) domain on its p66 subunit that can be expressed as a stable, although inactive protein. Recent studies of several RH enzymes demonstrate that substrate binding plays a major role in the creation of the active site. In the absence of substrate, the C-terminal helix E of the RT RNase H domain is dynamic, characterized by severe exchange broadening of its backbone amide resonances, so that the solution characterization of this region of the protein has been limited. Nuclear magnetic resonance studies of 13C-labeled RH as a function of experimental conditions reveal that the δ1 methyl resonance of Ile556, located in a short, random coil segment following helix E, experiences a large 13C shift corresponding to a conformational change of Ile556 that results from packing of helix E against the central β-sheet. This shift provides a useful basis for monitoring the effects of various ligands on active site formation. Additionally, we report that the RNase H complexes formed with one or both divalent ions can be individually observed and characterized using diamagnetic Zn2+ as a substitute for Mg2+. Ordering of helix E results specifically from the interaction with the lower affinity binding to the A divalent ion site.
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