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Reverse transcriptase
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== Structure == The reverse transcriptase employs a "right hand" structure similar to that found in other [[RNA-dependent RNA polymerase|viral nucleic acid polymerase]]s.<ref name="pmid19022262"/><ref name="pmid9309225">{{cite journal | vauthors = Hansen JL, Long AM, Schultz SC | title = Structure of the RNA-dependent RNA polymerase of poliovirus | journal = Structure | volume = 5 | issue = 8 | pages = 1109β22 | date = August 1997 | pmid = 9309225 | doi = 10.1016/S0969-2126(97)00261-X | doi-access = free }}</ref> In addition to the transcription function, retroviral reverse transcriptases have a domain belonging to the [[RNase H]] family, which is vital to their replication. By degrading the RNA template, it allows the other strand of DNA to be synthesized.<ref>{{cite journal | vauthors = Schultz SJ, Champoux JJ | title = RNase H activity: structure, specificity, and function in reverse transcription | journal = Virus Research | volume = 134 | issue = 1β2 | pages = 86β103 | date = June 2008 | pmid = 18261820 | pmc = 2464458 | doi = 10.1016/j.virusres.2007.12.007 }}</ref> Some fragments from the digestion also serve as the primer for the [[DNA polymerase]] (either the same enzyme or a host protein), responsible for making the other (plus) strand.<ref name="pmid19022262">{{cite journal | vauthors = Sarafianos SG, Marchand B, Das K, Himmel DM, Parniak MA, Hughes SH, Arnold E | title = Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition | journal = Journal of Molecular Biology | volume = 385 | issue = 3 | pages = 693β713 | date = January 2009 | pmid = 19022262 | pmc = 2881421 | doi = 10.1016/j.jmb.2008.10.071 }}</ref>
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