| Literature DB >> 7498546 |
Abstract
A non-structural protein of the hepatitis C virus (HCV), NS3, contains amino acid sequence motifs characteristic of serine-proteinases and RNA helicases. RNA binding activity of the NS3 protein with an apparent dissociation constant of 2 x 10(-7) M was detected using a poly(U)-Sepharose resin. Competitive RNA binding analysis suggested that the NS3 protein binds preferentially to the poly(U) sequence, which is located at the 3' end of HCV RNA. Mutational analysis of NS3 protein revealed the possibility that both the RNA helicase region and the serine-proteinase region were necessary for full RNA binding activity.Entities:
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Year: 1995 PMID: 7498546 DOI: 10.1016/0014-5793(95)01283-x
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124