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Mechanism of auxin perception by the TIR1 ubiquitin ligase

cflikunlun 添加于 2011-1-9 20:43 | 1428 次阅读 | 0 个评论
  •  作 者

    Tan X, Calderon-Villalobos LIA, Sharon M, Zheng C, Robinson CV, Estelle M, Zheng N
  •  摘 要

    Auxin is a pivotal plant hormone that controls many aspects of plant growth and development. Perceived by a small family of F-box proteins including transport inhibitor response 1 (TIR1), auxin regulates gene expression by promoting SCF ubiquitin-ligase-catalysed degradation of the Aux/IAA transcription repressors, but how the TIR1 F-box protein senses and becomes activated by auxin remains unclear. Here we present the crystal structures of the Arabidopsis TIR1-ASK1 complex, free and in complexes with three different auxin compounds and an Aux/IAA substrate peptide. These structures show that the leucine-rich repeat domain of TIR1 contains an unexpected inositol hexakisphosphate co-factor and recognizes auxin and the Aux/IAA polypeptide substrate through a single surface pocket. Anchored to the base of the TIR1 pocket, auxin binds to a partially promiscuous site, which can also accommodate various auxin analogues. Docked on top of auxin, the Aux/IAA substrate peptide occupies the rest of the TIR1 pocket and completely encloses the hormone-binding site. By filling in a hydrophobic cavity at the protein interface, auxin enhances the TIR1-substrate interactions by acting as a 'molecular glue'. Our results establish the first structural model of a plant hormone receptor.
  •  详细资料

    • 文献种类:期刊
    • 期刊名称: Nature
    • 期刊缩写: Nature
    • 期卷页: 2007  446 7136 640-645
    • 地址: Department of Pharmacology, University of Washington, School of Medicine, Box 357280, Seattle, Washington 98195, USA
    • ISBN: 0028-0836
    • 备注:PMID:17410169
  • 相关链接 DOI URL 

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