Structural Studies of Peptide Binding Interaction of HCV IRES Domain IV

Title
Structural Studies of Peptide Binding Interaction of HCV IRES Domain IV
Authors
김낙균방경미신지연송현규
Keywords
HCV IRES; HCV IRES domain IV; RNA structure; RNA binding peptide; NMR
Issue Date
2017-09
Publisher
Journal of the Korean Magnetic Resonance Society
Citation
VOL 21-113
Abstract
The hepatitis C virus (HCV) internal ribosome entry site (IRES) is an RNA structure located in the 5’-UTR of the HCV RNA genome. The HCV IRES consists of four domains I, II, III, and IV, where domains II - IV are recognized by 40S ribosomal subunit and the domain III is bound to eukaryotic initiation factor 3 (eIF3) for translation initiation. Here, we have characterized the tertiary interaction between an L-/K- rich peptide and the HCV IRES domain IV. To probe the peptide binding interface in RNA, we synthesized 13C- and 15N- double labeled RNA and the binding site was identified by using the chemical shift perturbation (CSP) NMR methods. Our results showed that the peptide binds to the upper stem of the IRES domain IV, indicating that the tertiary interaction between the IRES domain IV and the peptide would disrupt the initiation of translation of HCV mRNA by blocking the start codon exposure. This study will provide an insight into the new peptide-based anti-viral drug design targeting HCV IRES RNA.
URI
http://pubs.kist.re.kr/handle/201004/66719
ISSN
1226-6531
Appears in Collections:
KIST Publication > Article
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