The β1′−β2′ Motif of the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Is Responsible for Conferring Open Conformation to the p66 Subunit by Displacing the Connection Domain from the Polymerase Cleft-Reference-Cited by-同舟云学术

The β1′−β2′ Motif of the RNase H Domain of Human Immunodeficiency Virus Type 1 Reverse Transcriptase Is Responsible for Conferring Open Conformation to the p66 Subunit by Displacing the Connection Domain from the Polymerase Cleft

Published:2017-06-28 Issue:27 Volume:56 Page:3434-3442
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Pandey Ashutosh K¹,Dixit Updesh¹,Kholodovych Vlad²³^ORCID,Comollo Thomas W.¹,Pandey Virendra N.¹^ORCID

Affiliation:

1. Department of Microbiology, Biochemistry and Molecular Genetics, New Jersey Medical School, Rutgers University-Newark, Newark, New Jersey 07103, United States

2. Office of Advanced Research Computing, Rutgers University, Piscataway, New Jersey 08854, United States

3. Department of Pharmacology, Robert Wood Johnson Medical School, Rutgers University, Piscataway, New Jersey 08854, United States

Funder

NIH Office of the Director

National Institute of Allergy and Infectious Diseases

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.7b00005

Reference42 articles.

1. Characterization of the human immunodeficiency virus type-1 reverse transcriptase enzyme produced in yeast

2. Biosynthesis and analysis of a genetically engineered HIV-1 reverse transcriptase/endonuclease polyprotein in Escherichia coli

3. Processing protease and reverse transcriptase from human immunodeficiency virus type I polyprotein in Escherichia coli

4. Reverse transcriptase of human immunodeficiency virus type 1: functionality of subunits of the heterodimer in DNA synthesis

5. Subunit-selective mutagenesis indicates minimal polymerase activity in heterodimer-associated p51 HIV-1 reverse transcriptase.

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