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

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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: Kim, Ju Hee; Kang, Sunghyun; Jung, Suk-Kyeong; Yu, Keum Ran; Chung, Sang J.; Chung, Bong Hyun; Erikson, Raymond Leo; Kim, Bo Yeon; Kim, Seung Jun

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Citation: Kim, Ju Hee, Sunghyun Kang, Suk-Kyeong Jung, Keum Ran Yu, Sang J. Chung, Bong Hyun Chung, Raymond L. Erikson, Bo Yeon Kim, and Seung Jun Kim. 2012. Crystal structure of xenotropic murine leukaemia virus-related virus (xmrv) ribonuclease h. Bioscience Reports 32(Pt 5): 455-463.
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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.
Published Version: doi:10.1042/BSR20120028
Other Sources: http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3475449/pdf/
Terms of Use: This article is made available under the terms and conditions applicable to Other Posted Material, as set forth at http://nrs.harvard.edu/urn-3:HUL.InstRepos:dash.current.terms-of-use#LAA
Citable link to this page: http://nrs.harvard.edu/urn-3:HUL.InstRepos:11729584
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