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摘要:Various aerolysin-like pore-forming proteins have been identified from bacteria to vertebrates. However, mechanisms of receptor recognition and/or pore formation of the eukaryotic members remain unknown. Here we present the first couple of structures of a vertebrate aerolysin-like protein from Danio rerio, termed Dln1, before and after pore formation. Each subunit of Dln1 dimer comprises a β-prism lectin module followed by an aerolysin module. Specific binding of the lectin module towards high-mannose glycans triggers drastic conformational changes of the aerolysin module in a p H-dependent manner, ultimately resulting in the formation of a membrane-bound octameric pore. Structural analyses combined with computational simulations and biochemical assays suggest a pore-forming process with an activation mechanism distinct from the previously characterized bacterial members. Moreover, Dln1 and its homologs are ubiquitously distributed in bony fishes and lamprey, suggesting a novel fish-specific defense molecule.
会议名称:

第十四次中国暨国际生物物理大会(ICBC2015)

会议时间:

2015-11-16

会议地点:

中国云南昆明

  • 专辑:

    基础科学

  • 专题:

    生物学

  • 分类号:

    Q51

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