Reverse transcriptase: Difference between revisions
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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> | ||
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==Structure== | ==Structure== | ||
This ''hand-like'' <scene name='Reverse_transcriptase/Chains/2'>heterodimer</scene> protein has an usual length of 1000 residues (560 in Chain A and 440 for B), a third of them involved in alpha helices and almost a quarter involved in beta sheets, showing α+β <scene name='Reverse_transcriptase/Secondary/2'>secondary structure</scene> domains. <scene name='Reverse_transcriptase/Chaina/2'>Chain A</scene> has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/2'>Chain B</scene> is around 51KDa. These monomers are derived from the same gene, but p51 lacks the amino acids of one active site and has a different tertiary structure conformation compared to p66. Because of this, p51 is enzymatically inactive. <ref>PMID: 1377403</ref> <!-- [http://www.sciencemag.org.silk.library.umass.edu:2048/cgi/content/abstract/sci;256/5065/1783?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&andorexacttitleabs=and&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&volume=256&firstpage=1783&resourcetype=HWCIT] --> | This ''hand-like'' <scene name='Reverse_transcriptase/Chains/2'>heterodimer</scene> protein has an usual length of 1000 residues (560 in Chain A and 440 for B), a third of them involved in alpha helices and almost a quarter involved in beta sheets, showing α+β <scene name='Reverse_transcriptase/Secondary/2'>secondary structure</scene> domains. <scene name='Reverse_transcriptase/Chaina/2'>Chain A</scene> has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/2'>Chain B</scene> is around 51KDa. These monomers are derived from the same gene, but p51 lacks the amino acids of one active site and has a different tertiary structure conformation compared to p66. Because of this, p51 is enzymatically inactive. <ref>PMID: 1377403</ref> <!-- [http://www.sciencemag.org.silk.library.umass.edu:2048/cgi/content/abstract/sci;256/5065/1783?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&andorexacttitleabs=and&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&volume=256&firstpage=1783&resourcetype=HWCIT] --> | ||
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</StructureSection> | </StructureSection> | ||
== 3D Structures of Reverse transcriptase == | == 3D Structures of Reverse transcriptase == | ||
