Reverse transcriptase: Difference between revisions
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[[Reverse transcriptase]] (RT) or RNA-dependent DNA polymerase transcribes single-stranded RNA into double-stranded [[DNA]]. HIV-1 RT is from the human immunodeficiency virus and is a heterodimer of P66 and P51 subchains. The images at the left and at the right correspond to one representative RT structure, ''i.e.'' crystal structure of HIV-1 Reverse transcriptase ([[1hmv]]). There are more details on HIV-1 RT in [[Phl p 2]]. P15 is its RNAse H domain. There are two types of inhibitors for RT: NNRTIs are the non-nucleoside inhibitors, and NRTIs are the nucleoide inhibitors. Being the protein that gives their name to Retroviruses, Reverse Transcriptase is, along with [[Hiv protease|Protease]] and Integrase, the most important part of the protein system involved in the process of infection and reproduction for viruses like HIV, MuLV and AMV. RT has the unusual property of transcribing ssRNA into dsDNA going against the Central Dogma of Molecular Biology. | [[Reverse transcriptase]] (RT) or RNA-dependent DNA polymerase transcribes single-stranded RNA into double-stranded [[DNA]]. HIV-1 RT is from the human immunodeficiency virus and is a heterodimer of P66 and P51 subchains. The images at the left and at the right correspond to one representative RT structure, ''i.e.'' crystal structure of HIV-1 Reverse transcriptase ([[1hmv]]). There are more details on HIV-1 RT in [[Phl p 2]]. P15 is its RNAse H domain. There are two types of inhibitors for RT: NNRTIs are the non-nucleoside inhibitors, and NRTIs are the nucleoide inhibitors. Being the protein that gives their name to Retroviruses, Reverse Transcriptase is, along with [[Hiv protease|Protease]] and Integrase, the most important part of the protein system involved in the process of infection and reproduction for viruses like HIV, MuLV and AMV. RT has the unusual property of transcribing ssRNA into dsDNA going against the Central Dogma of Molecular Biology. | ||
Since its discovery in 1970, the study of its properties and mechanisms of action have been of high interest among the scientific community due to the unique properties that makes it an important medical target enzyme and important tool for genetic engineering applications like RT-PCR in the construction of cDNA libraries. See also [[Transcription and RNA Processing]] | Since its discovery in 1970, the study of its properties and mechanisms of action have been of high interest among the scientific community due to the unique properties that makes it an important medical target enzyme and important tool for genetic engineering applications like RT-PCR in the construction of cDNA libraries. See also <br /> | ||
[[Transcription and RNA Processing]]<br /> | |||
[[HIV-1 Reverse Transcriptase in Complex with Nevirapine]]<br /> | |||
[[AZT-resistant HIV-1 reverse transcriptase]]. | |||
Reverse Transcriptase is one of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. <scene name='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA'>-- CBI Molecular Playground Model --</scene> | Reverse Transcriptase is one of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. <scene name='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA'>-- CBI Molecular Playground Model --</scene> | ||