Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H
Kim, Ju Hee
Yu, Keum Ran
Chung, Sang J.
Chung, Bong Hyun
Kim, Bo Yeon
Kim, Seung JunNote: Order does not necessarily reflect citation order of authors.
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CitationKim, 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.
AbstractRNase 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.
Citable link to this pagehttp://nrs.harvard.edu/urn-3:HUL.InstRepos:11729584
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