Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Priyadarshi, Amit | - |
dc.contributor.author | Roy, Ankoor | - |
dc.contributor.author | Kim, Key Sun | - |
dc.contributor.author | Kim, Eunice EunKyeong | - |
dc.contributor.author | Hwang, Kwang Yeon | - |
dc.date.accessioned | 2024-01-20T19:33:07Z | - |
dc.date.available | 2024-01-20T19:33:07Z | - |
dc.date.created | 2021-09-02 | - |
dc.date.issued | 2010-04 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.uri | https://pubs.kist.re.kr/handle/201004/131591 | - |
dc.description.abstract | This study reports the crystal structures of Bcl-xl wild type and three Bcl-xl mutants (Y101A, F105A, and R139A) with amino acid substitutions in the hydrophobic groove of the Bcl-xl BH3 domain An additional 12 ordered residues were observed in a highly flexible loop between the alpha 1 and alpha 2 helices, and were recognized as an important deamidation site for the regulation of apoptosis The autophagy-effector protein, Beclin 1, contains a novel BH3 domain (residues 101-125), which binds to the surface cleft of Bcl-xl, as confirmed by nuclear magnetic resonance (NMR) spectroscopy and analytical gel-filtration results Gossypol, a potent inhibitor of Bcl-xl, had a K-d value of 0 9 mu M In addition, the structural and biochemical analysis of five Bcl-xl substitution mutants will provide structural insights into the design and development of anti-cancer drugs (C) 2010 Elsevier Inc All rights reserved | - |
dc.language | English | - |
dc.publisher | Academic Press | - |
dc.title | Structural insights into mouse anti-apoptotic Bcl-xl reveal affinity for Beclin 1 and gossypol | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.bbrc.2010.03.002 | - |
dc.description.journalClass | 1 | - |
dc.identifier.bibliographicCitation | Biochemical and Biophysical Research Communications, v.394, no.3, pp.515 - 521 | - |
dc.citation.title | Biochemical and Biophysical Research Communications | - |
dc.citation.volume | 394 | - |
dc.citation.number | 3 | - |
dc.citation.startPage | 515 | - |
dc.citation.endPage | 521 | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.identifier.wosid | 000276785900015 | - |
dc.identifier.scopusid | 2-s2.0-77950518734 | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.type.docType | Article | - |
dc.subject.keywordPlus | CRYSTAL-STRUCTURE | - |
dc.subject.keywordPlus | PEPTIDE COMPLEX | - |
dc.subject.keywordPlus | REGULATORS | - |
dc.subject.keywordPlus | BCL-X(L) | - |
dc.subject.keywordPlus | RAY | - |
dc.subject.keywordAuthor | Bcl-xl | - |
dc.subject.keywordAuthor | Beclin | - |
dc.subject.keywordAuthor | Apoptosis | - |
dc.subject.keywordAuthor | Gossypol | - |
dc.subject.keywordAuthor | Mutation | - |
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