Sandbox Reserved 1688: Difference between revisions

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Motifs –

There are seven conserved structural motifs, A to G, throughout all RdRps. A to E are motifs present in the palm domain. Motif G and F are part of the fingers domain. Due to HCV being a positive RNA strand, it contains an additional motif termed H. The H motif is present in the thumb domain. Motif C, a heavily conserved motif, is formed by a loop and two flanking beta strands. The loop region is essential for binding the Mg2+ ions. Motif F is comprised of a loop and a beta strand. This motif interacts with the phosphate group of an incoming NTP. In HCV it is predicted to promote RNA synthesis. Motif G is a loop that is a part of the template strand entrance tunnel in HCV. Not including motifs H, F, and G, the remaining motifs are functionally conserved in NS5B protein in regards to a traditional RdRp.

There are seven conserved structural motifs, A to G, throughout all RdRps. A to E are motifs present in the palm domain. Motif G and F are part of the fingers domain. Due to HCV being a positive RNA strand, it contains an additional motif termed H. The H motif is present in the thumb domain. Motif C, a heavily conserved motif, is formed by a loop and two flanking beta strands. The loop region is essential for binding the Mg2+ ions. The conserved residues <scene name='89/891378/Conserved_asp/1'>Asp220, Asp319, and Asp318</scene> coordinate the metal ion. Motif F is comprised of a loop and a beta strand. This motif interacts with the phosphate group of an incoming NTP. In HCV it is predicted to promote RNA synthesis. Motif G is a loop that is a part of the template strand entrance tunnel in HCV. Not including motifs H, F, and G, the remaining motifs are functionally conserved in NS5B protein in regards to a traditional RdRp.

Catalytic Site –

Sandbox Reserved 1688: Difference between revisions

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 Motifs –
-There are seven conserved structural motifs, A to G, throughout all RdRps. A to E are motifs present in the palm domain. Motif G and F are part of the fingers domain. Due to HCV being a positive RNA strand, it contains an additional motif termed H. The H motif is present in the thumb domain. Motif C, a heavily conserved motif, is formed by a loop and two flanking beta strands. The loop region is essential for binding the Mg2+ ions. Motif F is comprised of a loop and a beta strand. This motif interacts with the phosphate group of an incoming NTP. In HCV it is predicted to promote RNA synthesis. Motif G is a loop that is a part of the template strand entrance tunnel in HCV. Not including motifs H, F, and G, the remaining motifs are functionally conserved in NS5B protein in regards to a traditional RdRp.
+There are seven conserved structural motifs, A to G, throughout all RdRps. A to E are motifs present in the palm domain. Motif G and F are part of the fingers domain. Due to HCV being a positive RNA strand, it contains an additional motif termed H. The H motif is present in the thumb domain. Motif C, a heavily conserved motif, is formed by a loop and two flanking beta strands. The loop region is essential for binding the Mg2+ ions. The conserved residues <scene name='89/891378/Conserved_asp/1'>Asp220, Asp319, and Asp318</scene> coordinate the metal ion. Motif F is comprised of a loop and a beta strand. This motif interacts with the phosphate group of an incoming NTP. In HCV it is predicted to promote RNA synthesis. Motif G is a loop that is a part of the template strand entrance tunnel in HCV. Not including motifs H, F, and G, the remaining motifs are functionally conserved in NS5B protein in regards to a traditional RdRp.
 Catalytic Site –