Reverse transcriptase: Difference between revisions

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==Structure==
==Structure==
This ''hand-like'' <scene name='Reverse_transcriptase/Chains/1'>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/1'>secondary structure</scene> domains; chain A has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/1'>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/1'>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/1'>secondary structure</scene> domains; <scene name='Reverse_transcriptase/Chaina/1'>Chain A</scene> has an usual weight of 66KDa whereas <scene name='Reverse_transcriptase/Chainb/1'>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]


==Function==
==Function==