Author: te Velthuis, Aartjan J.W.; van den Worm, Sjoerd H. E.; Snijder, Eric J.
Title: The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension Document date: 2011_10_29
ID: tx0lqgff_29
Snippet: When we next added an equimolar amount of nsp7 to the nsp8 RNA-binding mutant K58A, we observed a minor increase in the binding affinity for RNA (compare Figure 3B with 3E) . Mutant D52A, on the other hand, behaved similar to the wild-type protein ( Figure 3E ). Together, these results complement the observation that various positively charged nsp7 residues line the inside of the nsp8-scaffolded RNA binding channel (13) , and they provide the fir.....
Document: When we next added an equimolar amount of nsp7 to the nsp8 RNA-binding mutant K58A, we observed a minor increase in the binding affinity for RNA (compare Figure 3B with 3E) . Mutant D52A, on the other hand, behaved similar to the wild-type protein ( Figure 3E ). Together, these results complement the observation that various positively charged nsp7 residues line the inside of the nsp8-scaffolded RNA binding channel (13) , and they provide the first direct evidence for a functional role of nsp7 in the SARS-CoV nsp(7+8) structure.
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