Reverse transcriptase: Difference between revisions

As a RNA-dependent DNA Polymerase, Reverse Transcriptase is able to recognize the initial RNA, transcribe it to ssDNA, cleave the remaining RNA and then build up the dsDNA. To do this the protein has two active catalytic zones. Chain A has the <scene name='Reverse_transcriptase/Fingers/4'>Polymerase active site</scene> that consist of two ''finger-like'' domains: one of them recognizes the initial nucleic acid by h-bond interactions with phosphate groups of the side chains, then both domains make a conformational change closing the recognition hole to allow the second domain with the support a  <scene name='Reverse_transcriptase/Magnesium/2'>Magnesium ion</scene> coordination system to begin the transcription process adding the specific DNA nucleotides. This change is allowed by a <scene name='Reverse_transcriptase/Flexible/2'>flexible zone</scene> between the two previous domains; it is used as a common pharmaceutical target site in order to prevent the change and therefore inhibit activity. This zone is the only zone of Chain A that has non-conserved aminoacids, giving the virus more drug resistance<ref>Consurf Data Base DOI: 10.1002/ijch.201200096</ref>

  [http://consurfdb.tau.ac.il/chain_selection.php?pdb_ID=1JLB Link to Consurf Data Base for PDB Entry: 1JLB].