Sandbox Reserved 1683: Difference between revisions
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Influenza A utilizes its trimer subunits to bind the template strand: the host capped RNA is bound by the PB2 cap-binding domain, followed by the cleavage of the PA/P3 endonuclease domain.<ref>PMID:27396566</ref> As mentioned before, the cap-binding domain then rotates allowing the insertion of the 3' end of the capped RNA, and then initiation begins once GTP is added to the 3' end of the capped primer which has become templated by the second residue in the viral RNA template.<ref>PMID:27396566</ref> | Influenza A utilizes its trimer subunits to bind the template strand: the host capped RNA is bound by the PB2 cap-binding domain, followed by the cleavage of the PA/P3 endonuclease domain.<ref>PMID:27396566</ref> As mentioned before, the cap-binding domain then rotates allowing the insertion of the 3' end of the capped RNA, and then initiation begins once GTP is added to the 3' end of the capped primer which has become templated by the second residue in the viral RNA template.<ref>PMID:27396566</ref> | ||
Nucleotides are guided into the polymerase through the entry channel, which is made of highly conserved basic amino acids and consists of all three Influenza A RDRP subunits.<ref>PMID:27396566</ref> The <scene name='89/891373/Priming_loop/ | Nucleotides are guided into the polymerase through the entry channel, which is made of highly conserved basic amino acids and consists of all three Influenza A RDRP subunits.<ref>PMID:27396566</ref> The <scene name='89/891373/Priming_loop/3'>priming loop</scene> is especially important, as it is a beta-hairpin that protrudes from the PB1 thumb domain and has the role of supporting the sugar-base of the initiating nucleotide and it contains conserved residues such as PRO651 and ASP445-446.<ref>PMID:27396566</ref> | ||
== Conservation within Influenza A RDRP == | == Conservation within Influenza A RDRP == | ||
