Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3--creatine transition-state analogue complex
DC Field | Value | Language |
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dc.contributor.author | Bong, Seoung Min | - |
dc.contributor.author | Moon, Jin Ho | - |
dc.contributor.author | Nam, Ki Hyun | - |
dc.contributor.author | Lee, Ki Seog | - |
dc.contributor.author | Chi, Young Min | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2021-09-09T02:33:34Z | - |
dc.date.available | 2021-09-09T02:33:34Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2008-11-26 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/122383 | - |
dc.description.abstract | Creatine kinase is a member of the phosphagen kinase family, which catalyzes the reversible phosphoryl transfer reaction that occurs between ATP and creatine to produce ADP and phosphocreatine. Here, three structural aspects of human-brain-type-creatine-kinase (hBB-CK) were identified by X-ray crystallography: the ligand-free-form at 2.2 angstrom; the ADP-Mg2+, nitrate, and creatine complex (transition-state-analogue complex; TSAC); and the ADP-Mg2+-complex at 2.0 angstrom. The structures of ligand-bound hBB-CK revealed two different monomeric states in a single homodimer. One monomer is a closed form, either bound to TSAC or the ADP-Mg2+-complex, and the second monomer is an unliganded open form. These structural studies provide a detailed mechanism indicating that the binding of ADP-Mg2+ alone may trigger conformational changes in hBB-CK that were not observed with muscle-type-CK. (C) 2008 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 | CRYSTAL-STRUCTURE | - |
dc.subject | ALZHEIMERS | - |
dc.subject | ISOENZYMES | - |
dc.subject | CK | - |
dc.title | Structural studies of human brain-type creatine kinase complexed with the ADP-Mg2+-NO3--creatine transition-state analogue complex | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Moon, Jin Ho | - |
dc.contributor.affiliatedAuthor | Chi, Young Min | - |
dc.contributor.affiliatedAuthor | Hwang, Kwang Yeon | - |
dc.identifier.doi | 10.1016/j.febslet.2008.10.039 | - |
dc.identifier.scopusid | 2-s2.0-55749089541 | - |
dc.identifier.wosid | 000261235000021 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.582, no.28, pp.3959 - 3965 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 582 | - |
dc.citation.number | 28 | - |
dc.citation.startPage | 3959 | - |
dc.citation.endPage | 3965 | - |
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 | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | ALZHEIMERS | - |
dc.subject.keywordPlus | ISOENZYMES | - |
dc.subject.keywordPlus | CK | - |
dc.subject.keywordAuthor | Brain-type creatine kinase | - |
dc.subject.keywordAuthor | Shuttle system | - |
dc.subject.keywordAuthor | Energy homeostasis | - |
dc.subject.keywordAuthor | Crystal structure | - |
dc.subject.keywordAuthor | Creatine complex | - |
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