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Title 

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

Authors 

Ju Hee KimSunghyun KangS K JungKeum Ran YuSang Jeon ChungBong Hyun ChungR L EriksonBo Yeon KimSeung Jun Kim

Publisher 

Springer Verlag (Germany)

Issue Date 

2012

Citation 

Bioscience Reports, vol. 32, no. 5, pp. 455-463

Keywords 

Escherichia coliMurine leukaemia virusReverse transcriptaseRibonuclease HXenotropic murine leukaemia virus-related virus (XMRV)

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.

ISSN 

0144-8463

Link 

http://dx.doi.org/10.1042/BSR20120028

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2018-08-01


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