Literature DB >> 34861939

Retroviral RNase H: Structure, mechanism, and inhibition.

Tatiana V Ilina1, Teresa Brosenitsch1, Nicolas Sluis-Cremer2, Rieko Ishima3.   

Abstract

All retroviruses encode the enzyme, reverse transcriptase (RT), which is involved in the conversion of the single-stranded viral RNA genome into double-stranded DNA. RT is a multifunctional enzyme and exhibits DNA polymerase and ribonuclease H (RNH) activities, both of which are essential to the reverse-transcription process. Despite the successful development of polymerase-targeting antiviral drugs over the last three decades, no bona fide inhibitor against the RNH activity of HIV-1 RT has progressed to clinical evaluation. In this review article, we describe the retroviral RNH function and inhibition, with primary consideration of the structural aspects of inhibition.
Copyright © 2021 Elsevier Inc. All rights reserved.

Entities:  

Keywords:  Dynamics; HIV-1; Retrovirus; Reverse transcriptase; Ribonuclease H; Structure

Mesh:

Substances:

Year:  2021        PMID: 34861939      PMCID: PMC8994160          DOI: 10.1016/bs.enz.2021.07.007

Source DB:  PubMed          Journal:  Enzymes        ISSN: 1874-6047


  123 in total

Review 1.  Dimerization inhibitors of HIV-1 reverse transcriptase, protease and integrase: a single mode of inhibition for the three HIV enzymes?

Authors:  María-José Camarasa; Sonsoles Velázquez; Ana San-Félix; María-Jesús Pérez-Pérez; Federico Gago
Journal:  Antiviral Res       Date:  2006-06-28       Impact factor: 5.970

Review 2.  Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.

Authors:  Takashi Tadokoro; Shigenori Kanaya
Journal:  FEBS J       Date:  2009-02-18       Impact factor: 5.542

3.  Entire-Dataset Analysis of NMR Fast-Exchange Titration Spectra: A Mg2+ Titration Analysis for HIV-1 Ribonuclease H Domain.

Authors:  Ichhuk Karki; Martin T Christen; Justin Spiriti; Ryan L Slack; Masayuki Oda; Kenji Kanaori; Daniel M Zuckerman; Rieko Ishima
Journal:  J Phys Chem B       Date:  2016-12-05       Impact factor: 2.991

4.  Peptides Mimicking the β7/β8 Loop of HIV-1 Reverse Transcriptase p51 as "Hotspot-Targeted" Dimerization Inhibitors.

Authors:  Pedro A Sánchez-Murcia; Sonia de Castro; Carlos García-Aparicio; M Angeles Jiménez; Angela Corona; Enzo Tramontano; Nicolas Sluis-Cremer; Luis Menéndez-Arias; Sonsoles Velázquez; Federico Gago; María-José Camarasa
Journal:  ACS Med Chem Lett       Date:  2020-01-24       Impact factor: 4.345

5.  Stepwise analyses of metal ions in RNase H catalysis from substrate destabilization to product release.

Authors:  Marcin Nowotny; Wei Yang
Journal:  EMBO J       Date:  2006-04-06       Impact factor: 11.598

6.  Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48.

Authors:  S Kanaya; M Oobatake; Y Liu
Journal:  J Biol Chem       Date:  1996-12-20       Impact factor: 5.157

7.  A new generation of peptide-based inhibitors targeting HIV-1 reverse transcriptase conformational flexibility.

Authors:  Audrey Agopian; Edwige Gros; Gudrun Aldrian-Herrada; Nathalie Bosquet; Pascal Clayette; Gilles Divita
Journal:  J Biol Chem       Date:  2008-10-23       Impact factor: 5.157

8.  Tunable alignment of macromolecules by filamentous phage yields dipolar coupling interactions.

Authors:  M R Hansen; L Mueller; A Pardi
Journal:  Nat Struct Biol       Date:  1998-12

9.  Calcium inhibition of ribonuclease H1 two-metal ion catalysis.

Authors:  Edina Rosta; Wei Yang; Gerhard Hummer
Journal:  J Am Chem Soc       Date:  2014-02-18       Impact factor: 15.419

10.  Structures of HIV-1 RT-RNA/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA/DNA: insights into requirements for RNase H cleavage.

Authors:  Kalyan Das; Sergio E Martinez; Rajiv P Bandwar; Eddy Arnold
Journal:  Nucleic Acids Res       Date:  2014-05-31       Impact factor: 16.971

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  1 in total

1.  RNase HI Depletion Strongly Potentiates Cell Killing by Rifampicin in Mycobacteria.

Authors:  Abeer Al-Zubaidi; Chen-Yi Cheung; Gregory M Cook; George Taiaroa; Valerie Mizrahi; J Shaun Lott; Stephanie S Dawes
Journal:  Antimicrob Agents Chemother       Date:  2022-09-26       Impact factor: 5.938

  1 in total

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