Reverse transcriptase: Difference between revisions

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<applet  size='[450,338]' frame='true' align='right' name='Reverse Transcriptase scene='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA' />
<applet  size='[450,338]' frame='true' align='right' name='Reverse Transcriptase scene='Reverse_transcriptase/Presentation/3' caption='The hand-like two-enzymes-in-one protein that amazingly makes DNA from RNA' />
This ''hand-like'' <scene name='Reverse_transcriptase/Chains/2'>heterodimer</scene> protein that has an usual length of 1000 residues (560 in Chain A and 440 for B), the third of them involved in alpha helical and almost a quarter in beta sheets, showing &alpha;+&beta; <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, those monomers are derived from the same gen but p51 lacks the aminoacids of one active site and has a different tertiary structure conformation compared with p66, for this reason is totally inactive. [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 that has an usual length of 1000 residues (560 in Chain A and 440 for B), the third of them involved in alpha helical and almost a quarter in beta sheets, showing &alpha;+&beta; <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, those monomers are derived from the same gen but p51 lacks the aminoacids of one active site and has a different tertiary structure conformation compared with p66, for this reason is totally 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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==References==
==References==
<ref group='xtra'>PMID: 18464735</ref>
<references />
<references/>
*[1] Kohistaedt, L.A. ''et al''. Science. 256, 1783-1790 (1992) | [http://dx.doi.org/10.1126/science.1377403 doi:10.1126/science.1377403]
*[2] Consurf Server Data Base. Evolutionary conservation profile for Reverse Transcriptase PDB file 1JLB <!--accessed November 28, 2009-->
*[2] Consurf Server Data Base. Evolutionary conservation profile for Reverse Transcriptase PDB file 1JLB <!--accessed November 28, 2009-->
*[3] Abbondanzieri, E.A. ''et al''. Nature 453, 184-189 (2008) | [http://dx.doi.org/10.1038/nature06941 doi:10.1038/nature06941]
*[3] Abbondanzieri, E.A. ''et al''. Nature 453, 184-189 (2008) | [http://dx.doi.org/10.1038/nature06941 doi:10.1038/nature06941]  


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