Title |
The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding
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Published in |
Retrovirology, September 2012
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DOI | 10.1186/1742-4690-9-73 |
Pubmed ID | |
Authors |
Berit Leo, Kristian Schweimer, Paul Rösch, Maximilian J Hartl, Birgitta M Wöhrl |
Abstract |
The ribonuclease H (RNase H) domains of retroviral reverse transcriptases play an essential role in the replication cycle of retroviruses. During reverse transcription of the viral genomic RNA, an RNA/DNA hybrid is created whose RNA strand needs to be hydrolyzed by the RNase H to enable synthesis of the second DNA strand by the DNA polymerase function of the reverse transcriptase. Here, we report the solution structure of the separately purified RNase H domain from prototype foamy virus (PFV) revealing the so-called C-helix and the adjacent basic loop, which both were suggested to be important in substrate binding and activity. |
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