C-terminal dimerization of apo-cyclic AMP receptor protein validated in solution
DC Field | Value | Language |
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dc.contributor.author | Sim, Dae-Won | - |
dc.contributor.author | Choi, Jae Wan | - |
dc.contributor.author | Kim, Ji-Hun | - |
dc.contributor.author | Ryu, Kyoung-Seok | - |
dc.contributor.author | Kim, Myeongkyu | - |
dc.contributor.author | Yu, Hee-Wan | - |
dc.contributor.author | Jo, Ku-Sung | - |
dc.contributor.author | Kim, Eun-Hee | - |
dc.contributor.author | Seo, Min-Duk | - |
dc.contributor.author | Jeon, Young Ho | - |
dc.contributor.author | Lee, Bong-Jin | - |
dc.contributor.author | Kim, Young Pil | - |
dc.contributor.author | Won, Hyung-Sik | - |
dc.date.accessioned | 2021-09-03T07:50:48Z | - |
dc.date.available | 2021-09-03T07:50:48Z | - |
dc.date.created | 2021-06-16 | - |
dc.date.issued | 2017-04 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/83975 | - |
dc.description.abstract | Although cyclic AMP receptor protein (CRP) has long served as a typical example of effector-mediated protein allostery, mechanistic details into its regulation have been controversial due to discrepancy between the known crystal structure and NMR structure of apo-CRP. Here, we report that the recombinant protein corresponding to its C-terminal DNA-binding domain (CDD) forms a dimer. This result, together with structural information obtained in the present NMR study, is consistent with the previous crystal structure and validates its relevance also in solution. Therefore, our findings suggest that dissociation of the CDD may be critically involved in cAMP-induced allosteric activation of CRP. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | WILEY | - |
dc.subject | ESCHERICHIA-COLI | - |
dc.subject | ALLOSTERIC TRANSITION | - |
dc.subject | ACTIVATOR PROTEIN | - |
dc.subject | CRYSTAL-STRUCTURE | - |
dc.subject | DNA-BINDING | - |
dc.subject | CAMP | - |
dc.subject | CAP | - |
dc.subject | CRP | - |
dc.subject | IDENTIFICATION | - |
dc.subject | RESOLUTION | - |
dc.title | C-terminal dimerization of apo-cyclic AMP receptor protein validated in solution | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Jeon, Young Ho | - |
dc.identifier.doi | 10.1002/1873-3468.12613 | - |
dc.identifier.scopusid | 2-s2.0-85016506742 | - |
dc.identifier.wosid | 000400895100010 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.591, no.7, pp.1064 - 1070 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 591 | - |
dc.citation.number | 7 | - |
dc.citation.startPage | 1064 | - |
dc.citation.endPage | 1070 | - |
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 | ESCHERICHIA-COLI | - |
dc.subject.keywordPlus | ALLOSTERIC TRANSITION | - |
dc.subject.keywordPlus | ACTIVATOR PROTEIN | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | DNA-BINDING | - |
dc.subject.keywordPlus | CAMP | - |
dc.subject.keywordPlus | CAP | - |
dc.subject.keywordPlus | CRP | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | RESOLUTION | - |
dc.subject.keywordAuthor | cyclic AMP receptor protein | - |
dc.subject.keywordAuthor | NMR spectroscopy | - |
dc.subject.keywordAuthor | protein allostery | - |
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