Download MendeleyThe solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding.
Leo, B., Schweimer, K., Rosch, P., Hartl, M.J., Wohrl, B.M.(2012) Retrovirology 9: 73-73
- PubMed: 22962864
- DOI: https://doi.org/10.1186/1742-4690-9-73
- Primary Citation of Related Structures:
2LSN - PubMed 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.
Organizational Affiliation:
Universität Bayreuth, Lehrstuhl Biopolymere, Universitätsstr, 30, D-95447 Bayreuth, Germany.
