Author: Zivcec, Marko; Scholte, Florine E. M.; Spiropoulou, Christina F.; Spengler, Jessica R.; Bergeron, Éric
Title: Molecular Insights into Crimean-Congo Hemorrhagic Fever Virus Document date: 2016_4_21
ID: 0a20s62q_21
Snippet: Oligomerization appears to regulate NP function. In the absence of RNA, NP appears to exist exclusively as a monomer; in this state, NP binds RNA weakly [66, 67] , suggesting that only NP oligomers effectively bind RNA. Additionally, comparing monomeric and oligomeric NP organization shows that the arm domain changes conformation upon oligomerization allowing stronger binding to RNA [73] . The nature of the chemical bonds between RNA and NP remai.....
Document: Oligomerization appears to regulate NP function. In the absence of RNA, NP appears to exist exclusively as a monomer; in this state, NP binds RNA weakly [66, 67] , suggesting that only NP oligomers effectively bind RNA. Additionally, comparing monomeric and oligomeric NP organization shows that the arm domain changes conformation upon oligomerization allowing stronger binding to RNA [73] . The nature of the chemical bonds between RNA and NP remain unknown, as the RNA structure has yet to be resolved in any of the NP models. However, mutating three CCHFV NP residues (K132, Q300, K411) predicted to bind RNA blocked the transcription and replication of CCHFV minigenomes [65, 67] .
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