Structural insight into the constitutive repression function of the nuclear receptor Rev-erbβ

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dc.contributor.authorEui-jeon Woo-
dc.contributor.authorDae Gwin Jeong-
dc.contributor.authorM Y Lim-
dc.contributor.authorSeung Jun Kim-
dc.contributor.authorK J Kim-
dc.contributor.authorSei Mee Yoon-
dc.contributor.authorByoung Chul Park-
dc.contributor.authorSeong Eon Ryu-
dc.date.accessioned2017-04-19T09:08:16Z-
dc.date.available2017-04-19T09:08:16Z-
dc.date.issued2007-
dc.identifier.issn0022-2836-
dc.identifier.uri10.1016/j.jmb.2007.08.037ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8105-
dc.description.abstractThe Rev-erb family is an orphan nuclear receptor acting as a negative regulator of transcription. Rev-erbα and Rev-erbβ are crucial components of the circadian clock and involved in various lipid homeostasis. They are unique nuclear receptors that lack the activation function 2 helix (AF2-helix) required for ligand-dependent activation by other members of nuclear receptors. Here, we report the crystal structure of Rev-erbβ (NR1D2) in a dimeric arrangement. The putative ligand-binding pocket (LBP) of Rev-erbβ is filled with bulky hydrophobic residues resulting in a residual cavity size that is too small to allow binding of any known ligand molecules. However, an alternative conformation of the putative LBP observed in another crystal form suggests the flexibility of this region. The kinked conformation of helix H11 allows helix H11 to bend toward helix H3 over the putative ligand binding pocket by filling and closing the cavity with its side-chains. In the absence of the AF2-helix and a cognate ligand, Rev-erbβ appears to stabilize the hydrophobic cluster in the putative ligand binding pocket and provide a structural platform for co-repressor binding by adopting the unique geometry of helix H11, a suitable conformation for the constitutive repression activity.-
dc.publisherElsevier-
dc.titleStructural insight into the constitutive repression function of the nuclear receptor Rev-erbβ-
dc.title.alternativeStructural insight into the constitutive repression function of the nuclear receptor Rev-erbβ-
dc.typeArticle-
dc.citation.titleJournal of Molecular Biology-
dc.citation.number3-
dc.citation.endPage744-
dc.citation.startPage735-
dc.citation.volume373-
dc.contributor.affiliatedAuthorEui-jeon Woo-
dc.contributor.affiliatedAuthorDae Gwin Jeong-
dc.contributor.affiliatedAuthorSeung Jun Kim-
dc.contributor.affiliatedAuthorSei Mee Yoon-
dc.contributor.affiliatedAuthorByoung Chul Park-
dc.contributor.affiliatedAuthorSeong Eon Ryu-
dc.contributor.alternativeName우의전-
dc.contributor.alternativeName정대균-
dc.contributor.alternativeName임미연-
dc.contributor.alternativeName김승준-
dc.contributor.alternativeName김경진-
dc.contributor.alternativeName윤세미-
dc.contributor.alternativeName박병철-
dc.contributor.alternativeName류성언-
dc.identifier.bibliographicCitationJournal of Molecular Biology, vol. 373, no. 3, pp. 735-744-
dc.identifier.doi10.1016/j.jmb.2007.08.037-
dc.subject.keywordconstitutive repression-
dc.subject.keywordcrystal structure-
dc.subject.keywordligand binding domain-
dc.subject.keywordorphan receptor-
dc.subject.keywordRev-erbβ-
dc.subject.localconstitutive repression-
dc.subject.localcrystal structure-
dc.subject.localCrystal structure-
dc.subject.localligand binding domain-
dc.subject.localorphan receptors-
dc.subject.localorphan receptor-
dc.subject.localRev-erbβ-
dc.description.journalClassY-
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
Division of Research on National Challenges > Bionanotechnology Research Center > 1. Journal Articles
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
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