Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded
Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a no...
| Main Authors: | , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2012
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| Online Access: | https://hdl.handle.net/10356/94173 http://hdl.handle.net/10220/7474 |
| _version_ | 1826112715752472576 |
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| author | Liang, Yu Ye, Hong Kang, Cong Bao Yoon, Ho Sup |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Liang, Yu Ye, Hong Kang, Cong Bao Yoon, Ho Sup |
| author_sort | Liang, Yu |
| collection | NTU |
| description | Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone 1H, 13C, and 15N resonances, 3JHNα coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. |
| first_indexed | 2024-10-01T03:11:20Z |
| format | Journal Article |
| id | ntu-10356/94173 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T03:11:20Z |
| publishDate | 2012 |
| record_format | dspace |
| spelling | ntu-10356/941732020-03-07T12:18:16Z Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded Liang, Yu Ye, Hong Kang, Cong Bao Yoon, Ho Sup School of Biological Sciences DRNTU::Science::Biological sciences::Microbiology::Virology Nonstructural protein 5A protein (NS5A) of hepatitis C virus (HCV) plays an important role in the regulation of viral replication, interferon resistance, and apoptosis. HCV NS5A comprises three domains. Recently the structure of domain 1 has been determined, revealing a structural scaffold with a novel zinc-binding motif and a disulfide bond. At present, the structures of domains 2 and 3 remain undefined. Domain 2 of HCV NS5A (NS5A-D2) is important for functions of NS5A and involved in molecular interactions with its own NS5B and PKR, a cellular interferon-inducible serine/threonine specific protein kinase. In this study we performed structural analysis of domain 2 by multinuclear nuclear magnetic resonance (NMR) spectroscopy. The analysis of the backbone 1H, 13C, and 15N resonances, 3JHNα coupling constants ,and 3D NOE data indicates that NS5A-D2 lacks secondary structural elements and reveals characteristics of unfolded proteins. NMR relaxation parameters confirmed the lack of rigid structure in the domain. The absence of an ordered conformation and the observation of a highly dynamic behavior of NS5A-D2 may provide an underlying molecular basis on its physiological function to allow NS5A-D2 to interact with a variety of biological partners. 2012-01-26T01:09:41Z 2019-12-06T18:51:59Z 2012-01-26T01:09:41Z 2019-12-06T18:51:59Z 2007 2007 Journal Article Liang, Y., Ye, H., Kang, C. B., & Yoon, H. S. (2007). Domain 2 of Nonstructural Protein 5A (NS5A) of Hepatitis C Virus Is Natively Unfolded. Biochemistry, 46(41), 11550-11558. https://hdl.handle.net/10356/94173 http://hdl.handle.net/10220/7474 10.1021/bi700776e en Biochemistry © 2007 American Chemical Society. |
| spellingShingle | DRNTU::Science::Biological sciences::Microbiology::Virology Liang, Yu Ye, Hong Kang, Cong Bao Yoon, Ho Sup Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title | Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title_full | Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title_fullStr | Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title_full_unstemmed | Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title_short | Domain 2 of non-structural protein 5A (NS5A) of hepatitis C virus is natively unfolded |
| title_sort | domain 2 of non structural protein 5a ns5a of hepatitis c virus is natively unfolded |
| topic | DRNTU::Science::Biological sciences::Microbiology::Virology |
| url | https://hdl.handle.net/10356/94173 http://hdl.handle.net/10220/7474 |
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