Solution Structure of the RNase H Domain of the HIV-1 Reverse Transcriptase in the Presence of Magnesium-Reference-Cited by-同舟云学术

Solution Structure of the RNase H Domain of the HIV-1 Reverse Transcriptase in the Presence of Magnesium

Published:2003-01-01 Issue:3 Volume:42 Page:639-650
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Pari Koteppa¹,Mueller Geoffrey A.¹,DeRose Eugene F.¹,Kirby Thomas W.¹,London Robert E.¹

Affiliation:

1. Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, P.O. Box 12233, Research Triangle Park, North Carolina 27709

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0204894

Reference53 articles.

1. Point mutations in conserved amino acid residues within the C-terminal domain of HIV-1 reverse transcriptase specifically repress RNase H function

2. HIV-1 RT-associated ribonuclease H displays both endonuclease and 3′----5′ exonuclease activity.

3. Purification and characterization of the RNase H domain of HIV-1 reverse transcriptase expressed in recombinantEscherichia coli

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