Selected article for: "hexadecameric ring structure and ring structure"

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_3
    Snippet: In spite of this attractive model, however, many questions regarding CoV RNA synthesis remain unanswered thus far. For instance, it is unclear whether the homomeric form of nsp8, for which in vitro RdRp activity was previously documented (12) , actually occurs in vivo, as nsp8 was also shown to co-crystallize and form a unique hexadecameric ring-structure with the 10-kDa nsp7 subunit that resides immediately upstream in the replicase polyprotein .....
    Document: In spite of this attractive model, however, many questions regarding CoV RNA synthesis remain unanswered thus far. For instance, it is unclear whether the homomeric form of nsp8, for which in vitro RdRp activity was previously documented (12) , actually occurs in vivo, as nsp8 was also shown to co-crystallize and form a unique hexadecameric ring-structure with the 10-kDa nsp7 subunit that resides immediately upstream in the replicase polyprotein precursors (Figure 1 ) (13) . In a similar fashion, it is presently unknown whether the postulated double-stranded RNA (dsRNA) binding channel of this complex plays a role in the RdRp activity of nsp8 and whether this activity is influenced by nsp7, particularly given the observed low fidelity and low processivity of nsp8 (12) .

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