DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cheong, HK | ko |
dc.contributor.author | Park, JY | ko |
dc.contributor.author | Kim, EH | ko |
dc.contributor.author | Lee, C | ko |
dc.contributor.author | Kim, S | ko |
dc.contributor.author | Kim, Y | ko |
dc.contributor.author | Choi, Byong-Seok | ko |
dc.contributor.author | Cheong, C | ko |
dc.date.accessioned | 2013-03-03T23:01:41Z | - |
dc.date.available | 2013-03-03T23:01:41Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 2003-11 | - |
dc.identifier.citation | INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY, v.35, no.11, pp.1548 - 1557 | - |
dc.identifier.issn | 1357-2725 | - |
dc.identifier.uri | http://hdl.handle.net/10203/80831 | - |
dc.description.abstract | Human aspartyl-tRNA synthetase (hDRS) contains an extension at the N-terminus, which is involved in the transfer of Asp-tRNA to elongation factor alpha1 (EF1alpha). The structure of the N-terminal extension is critical to its function. Conformational studies on the synthetic, 21-residue N-terminal extension peptide (Thr(5)-Lys(25)) of human aspartyl-tRNA synthetase using H-1 nuclear magnetic resonance (NMR) spectroscopy, showed that the C-terminus adopts a regular alpha-helix with amphiphilicity, while the N-terminus shows a less-ordered structure with a flexible beta-turn. The observed characteristics suggest a structural switch model, such that when the tRNA is in the stretched conformation, the peptide reduces the rate of dissociation of Asp-tRNA from human aspartyl-tRNA synthetase, and provides enough time for elongation factor la to interact with the Asp-tRNA. Following Asp-tRNA transfer to EF1alpha, the peptide assumes the folded conformation. The structural switch model supports the direct transfer mechanism. (C) 2003 Elsevier Science Ltd. All rights reserved. | - |
dc.language | English | - |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | - |
dc.subject | AMINOACYL-TRANSFER-RNA | - |
dc.subject | ELONGATION-FACTOR 1-ALPHA | - |
dc.subject | AMPHIPHILIC HELIX | - |
dc.subject | COMPLETE SEQUENCE | - |
dc.subject | NMR-SPECTROSCOPY | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | PEPTIDE | - |
dc.subject | COMPLEX | - |
dc.subject | EXPRESSION | - |
dc.subject | INITIATION | - |
dc.title | Structure of the N-terminal extension of human aspartyl-tRNA synthetase: implications for its biological function | - |
dc.type | Article | - |
dc.identifier.wosid | 000184727500005 | - |
dc.identifier.scopusid | 2-s2.0-0038005312 | - |
dc.type.rims | ART | - |
dc.citation.volume | 35 | - |
dc.citation.issue | 11 | - |
dc.citation.beginningpage | 1548 | - |
dc.citation.endingpage | 1557 | - |
dc.citation.publicationname | INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | - |
dc.contributor.localauthor | Choi, Byong-Seok | - |
dc.contributor.nonIdAuthor | Cheong, HK | - |
dc.contributor.nonIdAuthor | Park, JY | - |
dc.contributor.nonIdAuthor | Kim, EH | - |
dc.contributor.nonIdAuthor | Lee, C | - |
dc.contributor.nonIdAuthor | Kim, S | - |
dc.contributor.nonIdAuthor | Kim, Y | - |
dc.contributor.nonIdAuthor | Cheong, C | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | DRS | - |
dc.subject.keywordAuthor | NMR structure | - |
dc.subject.keywordAuthor | multi-synthetase complex | - |
dc.subject.keywordAuthor | N-terminal extension | - |
dc.subject.keywordPlus | AMINOACYL-TRANSFER-RNA | - |
dc.subject.keywordPlus | ELONGATION-FACTOR 1-ALPHA | - |
dc.subject.keywordPlus | AMPHIPHILIC HELIX | - |
dc.subject.keywordPlus | COMPLETE SEQUENCE | - |
dc.subject.keywordPlus | NMR-SPECTROSCOPY | - |
dc.subject.keywordPlus | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | PEPTIDE | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | INITIATION | - |
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