The crystal structure of arginyl-tRNA synthetase from Homo sapiens
DC Field | Value | Language |
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dc.contributor.author | Kim, Hyun Sook | - |
dc.contributor.author | Cha, So Young | - |
dc.contributor.author | Jo, Chang Hwa | - |
dc.contributor.author | Han, Ahreum | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2021-09-05T07:37:03Z | - |
dc.date.available | 2021-09-05T07:37:03Z | - |
dc.date.created | 2021-06-15 | - |
dc.date.issued | 2014-06-27 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/98193 | - |
dc.description.abstract | Arginyl-tRNA synthetase (ArgRS) is a tRNA-binding protein that catalyzes the esterification of L-arginine to its cognate tRNA. L-Canavanine, a structural analog of L-arginine, has recently been studied as an anticancer agent. Here, we determined the crystal structures of the apo, L-arginine-complexed, and L-canavanine-complexed forms of the cytoplasmic free isoform of human ArgRS (hArgRS). Similar interactions were formed upon binding to L-canavanine or L-arginine, but the interaction between Tyr312 and the oxygen of the oxyguanidino group was a little bit different. Detailed conformational changes that occur upon substrate binding were explained. The hArgRS structure was also compared with previously reported homologue structures. The results presented here may provide a basis for the design of new anticancer drugs, such as L-canavanine analogs. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.subject | AMINOACYL-TRANSFER-RNA | - |
dc.subject | RIBONUCLEIC-ACID SYNTHETASE | - |
dc.subject | L-CANAVANINE | - |
dc.subject | 2 FORMS | - |
dc.subject | MECHANISM | - |
dc.subject | ACTIVATION | - |
dc.subject | PATHWAY | - |
dc.subject | DOMAIN | - |
dc.subject | ANALOG | - |
dc.title | The crystal structure of arginyl-tRNA synthetase from Homo sapiens | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.identifier.doi | 10.1016/j.febslet.2014.05.027 | - |
dc.identifier.scopusid | 2-s2.0-84902653809 | - |
dc.identifier.wosid | 000338401100022 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.588, no.14, pp.2328 - 2334 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 588 | - |
dc.citation.number | 14 | - |
dc.citation.startPage | 2328 | - |
dc.citation.endPage | 2334 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | AMINOACYL-TRANSFER-RNA | - |
dc.subject.keywordPlus | RIBONUCLEIC-ACID SYNTHETASE | - |
dc.subject.keywordPlus | L-CANAVANINE | - |
dc.subject.keywordPlus | 2 FORMS | - |
dc.subject.keywordPlus | MECHANISM | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | DOMAIN | - |
dc.subject.keywordPlus | ANALOG | - |
dc.subject.keywordAuthor | Arginyl-tRNA synthetase | - |
dc.subject.keywordAuthor | L-Canavanine | - |
dc.subject.keywordAuthor | L-Arginine | - |
dc.subject.keywordAuthor | Rossmann fold | - |
dc.subject.keywordAuthor | tRNA(Arg) | - |
dc.subject.keywordAuthor | Enzyme Commission number (6.1.1.19) | - |
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