Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H

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Title
Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H
Author(s)
Ju Hee Kim; Sunghyun Kang; S K Jung; Keum Ran Yu; Sang Jeon Chung; Bong Hyun Chung; R L Erikson; Bo Yeon KimSeung Jun Kim
Bibliographic Citation
Bioscience Reports, vol. 32, no. 5, pp. 455-463
Publication Year
2012
Abstract
RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA. In the present study we have determined the complete structure of the RNase H domain from XMRV (xenotropic murine leukaemia virus-related virus) RT (reverse transcriptase). The basic protrusion motif of the XMRV RNase H domain is folded as a short helix and an adjacent highly bent loop. Structural superposition and subsequent mutagenesis experiments suggest that the basic protrusion motif plays a role in direct binding to the major groove in RNA/DNA hybrid, as well as in establishing the co-ordination among modules in RT necessary for proper function.
Keyword
Escherichia coliMurine leukaemia virusReverse transcriptaseRibonuclease HXenotropic murine leukaemia virus-related virus (XMRV)
ISSN
0144-8463
Publisher
Portland Press Ltd
DOI
http://dx.doi.org/10.1042/BSR20120028
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Ochang Branch Institute > Anticancer Agent Research Center > 1. Journal Articles
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