DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, DW | ko |
dc.contributor.author | Gwack, Y | ko |
dc.contributor.author | Han, JH | ko |
dc.contributor.author | Choe, Joonho | ko |
dc.date.accessioned | 2013-03-03T06:12:58Z | - |
dc.date.available | 2013-03-03T06:12:58Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1997-05 | - |
dc.identifier.citation | VIRUS RESEARCH, v.49, no.1, pp.17 - 25 | - |
dc.identifier.issn | 0168-1702 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77580 | - |
dc.description.abstract | Hepatitis C virus (HCV) possesses two separate enzymatic functions in the NS3 protein: a protease and an NTPase/RNA helicase. In order to determine the minimal domain for NTPase and RNA helicase activities of the HCV NS3 protein, serial deletion mutants were constructed. The NS3H protein, a fusion protein of 25 amino acids (aa) from an expression vector and the C-terminal 466 aa of the HCV NS3 protein, contains an NTPase/RNA helicase activity. We made deletion mutants of 10, 30, 50, 97, and 135 aa from the C-terminus and 16 and 32 aa from the N-terminus of the NS3H protein. The deleted protein lacking: 50 aa from the C-terminus still possessed both activities, while the protein lacking 97 aa from the C-terminus lost an RNA helicase activity. The mutant lacking 16 amino acids from the N-terminus retained the enzymatic activities and the N-terminal 32 aa deleted mutant lost an NTPase/RNA helicase activity. A combinational deletion mutant lacking 16 aa the N-terminus and 50 aa from the C-terminus retained the enzymatic activities. These results show that the functional domain of the HCV NTPase/RNA helicase is about 400 aa in length and maps between NS3 residues 1209 and 1608. (C) 1997 Elsevier Science B.V. | - |
dc.language | English | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | MUTATIONAL ANALYSIS | - |
dc.subject | STIMULATED NTPASE | - |
dc.subject | P80 PROTEIN | - |
dc.subject | 3&apos | - |
dc.subject | END | - |
dc.subject | PESTIVIRUS | - |
dc.subject | REPLICATION | - |
dc.subject | FLAVIVIRUS | - |
dc.subject | SEQUENCES | - |
dc.subject | GENOME | - |
dc.subject | REGION | - |
dc.title | Towards defining a minimal functional domain for NTPase and RNA helicase activities of the hepatitis C virus NS3 protein | - |
dc.type | Article | - |
dc.identifier.wosid | A1997XC44300003 | - |
dc.identifier.scopusid | 2-s2.0-0342872087 | - |
dc.type.rims | ART | - |
dc.citation.volume | 49 | - |
dc.citation.issue | 1 | - |
dc.citation.beginningpage | 17 | - |
dc.citation.endingpage | 25 | - |
dc.citation.publicationname | VIRUS RESEARCH | - |
dc.contributor.localauthor | Choe, Joonho | - |
dc.contributor.nonIdAuthor | Kim, DW | - |
dc.contributor.nonIdAuthor | Gwack, Y | - |
dc.contributor.nonIdAuthor | Han, JH | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | HCV | - |
dc.subject.keywordAuthor | NS3 | - |
dc.subject.keywordAuthor | NTPase | - |
dc.subject.keywordAuthor | RNA helicase | - |
dc.subject.keywordPlus | MUTATIONAL ANALYSIS | - |
dc.subject.keywordPlus | STIMULATED NTPASE | - |
dc.subject.keywordPlus | P80 PROTEIN | - |
dc.subject.keywordPlus | 3&apos | - |
dc.subject.keywordPlus | END | - |
dc.subject.keywordPlus | PESTIVIRUS | - |
dc.subject.keywordPlus | REPLICATION | - |
dc.subject.keywordPlus | FLAVIVIRUS | - |
dc.subject.keywordPlus | SEQUENCES | - |
dc.subject.keywordPlus | GENOME | - |
dc.subject.keywordPlus | REGION | - |
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