Structure of the conserved domain of ANAC, a member of the NAC family of transcription factors
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- Heidi A Ernst
- Department of Chemistry, Centre for Crystallographic Studies, University of Copenhagen Copenhagen Ø Denmark
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- Addie Nina Olsen
- Institute of Molecular Biology, University of Copenhagen Copenhagen K Denmark
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- Karen Skriver
- Institute of Molecular Biology, University of Copenhagen Copenhagen K Denmark
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- Sine Larsen
- Department of Chemistry, Centre for Crystallographic Studies, University of Copenhagen Copenhagen Ø Denmark
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- Leila Lo Leggio
- Department of Chemistry, Centre for Crystallographic Studies, University of Copenhagen Copenhagen Ø Denmark
書誌事項
- 公開日
- 2004-02-13
- 権利情報
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- http://onlinelibrary.wiley.com/termsAndConditions#vor
- DOI
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- 10.1038/sj.embor.7400093
- 公開者
- Springer Science and Business Media LLC
この論文をさがす
説明
<jats:p> The structure of the DNA‐binding NAC domain of <jats:italic>Arabidopsis</jats:italic> ANAC (abscisic‐acid‐responsive NAC) has been determined by X‐ray crystallography to 1.9 Å resolution (Protein Data Bank codes 1UT4 and 1UT7). This is the first structure determined for a member of the NAC family of plant‐specific transcriptional regulators. NAC proteins are characterized by their conserved N‐terminal NAC domains that can bind both DNA and other proteins. NAC proteins are involved in developmental processes, including formation of the shoot apical meristem, floral organs and lateral shoots, as well as in plant hormonal control and defence. The NAC domain does not possess a classical helix–turn–helix motif; instead it reveals a new transcription factor fold consisting of a twisted β‐sheet surrounded by a few helical elements. The functional dimer formed by the NAC domain was identified in the structure, which will serve as a structural template for understanding NAC protein function at the molecular level. </jats:p>
収録刊行物
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- EMBO reports
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EMBO reports 5 (3), 297-303, 2004-02-13
Springer Science and Business Media LLC
