ArticleJournal of virology2006
Crystal structure of the moloney murine leukemia virus RNase H domain.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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Who cites it
29 citing papers in PubMed, 62 citations in OpenAlex.
- Article
- Enhancing thermostability of Moloney murine leukemia virus reverse transcriptase through greedy combination of multiple mutant residues.Bioresources and bioprocessing · 2025Article
- Developing, Characterizing, and Modeling CRISPR-Based Point-of-Use Pathogen Diagnostics.ACS synthetic biology · 2025Article
- Developing, characterizing and modeling CRISPR-based point-of-use pathogen diagnostics.bioRxiv : the preprint server for biology · 2024Article
- An engineered prime editor with enhanced editing efficiency in plants.Nature biotechnology · 2022Article
- A second hybrid-binding domain modulates the activity of Drosophila ribonuclease H1.Journal of biochemistry · 2020Article
- RNA sequencing by direct tagmentation of RNA/DNA hybrids.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Genetic encoding of DNA nanostructures and their self-assembly in living bacteria.Nature communications · 2016Article
- Ultradeep pyrosequencing and molecular modeling identify key structural features of hepatitis B virus RNase H, a putative target for antiviral intervention.Journal of virology · 2014Article
- Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid.Nucleic acids research · 2013Article
- Structural basis of the allosteric inhibitor interaction on the HIV-1 reverse transcriptase RNase H domain.Chemical biology & drug design · 2012Article
- Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H.Bioscience reports · 2012Article
- The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.Retrovirology · 2012Article
- Structural and inhibition studies of the RNase H function of xenotropic murine leukemia virus-related virus reverse transcriptase.Antimicrobial agents and chemotherapy · 2012Article
- Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus.Journal of structural biology · 2012Article
- Insights into the structure and activity of prototype foamy virus RNase H.Retrovirology · 2012Article
- Bleach gel: a simple agarose gel for analyzing RNA quality.Electrophoresis · 2012Article
- Retroviral reverse transcriptases.Cellular and molecular life sciences : CMLS · 2010Review
- Structural and functional characterization of an RNase HI domain from the bifunctional protein Rv2228c from Mycobacterium tuberculosis.Journal of bacteriology · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
A crystallographic study of the Moloney murine leukemia virus (Mo-MLV) RNase H domain was performed to provide information about its structure and mechanism of action. These efforts resulted in the crystallization of a mutant Mo-MLV RNase H lacking the putative helix C (DeltaC). The 1.6-Angstroms resolution structure resembles the known structures of the human immunodeficiency virus type 1 (HIV-1) and Escherichia coli RNase H. The structure revealed the coordination of a magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583. Surface charge mapping of the Mo-MLV structure revealed a high density of basic charges on one side of the enzyme. Using a model of the Mo-MLV structure superimposed upon a structure of HIV-1 reverse transcriptase bound to an RNA/DNA hybrid substrate, Mo-MLV RNase H secondary structures and individual amino acids were examined for their potential roles in binding substrate. Identified regions included Mo-MLV RNase H beta1-beta2, alphaA, and alphaB and residues from alphaB to alphaD and its following loop. Most of the identified substrate-binding residues corresponded with residues directly binding nucleotides in an RNase H from Bacillus halodurans as observed in a cocrystal structure with RNA/DNA. Finally, superimposition of RNases H of Mo-MLV, E. coli, and HIV-1 revealed that a loop of the HIV-1 connection domain resides within the same region of the Mo-MLV and E. coli C-helix. The HIV-1 connection domain may serve to recognize and bind the RNA/DNA substrate major groove.
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Registered trials
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