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Abstract

Laminins regulate diverse cellular functions through interaction with integrins. Two regions of laminins—three laminin globular domains of the α chain (LG1–3) and the carboxyl-terminal tail of the γ chain (γ-tail)—are required for integrin binding, but it remains unclear how the γ-tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the γ-tail extends to the bottom face of LG1–3. Electron microscopic imaging combined with biochemical analyses showed that integrin binds to the bottom face of LG1–3 with the γ1-tail apposed to the metal ion–dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the γ-tail coordinates the metal ion in the MIDAS through its Glu residue.

Mamoru Takizawa, Takao Arimori, Yukimasa Taniguchi, Yu Kitago, Erika Yamashita, Junichi Takagi and Kiyotoshi Sekiguchi, "Mechanistic basis for the recognition of laminin-511 by α6β1 integrin", Science Advances, Vol. 3, No. 9, e1701497, AAAS, 2017

Journal

  • Science Advances

    Science Advances 3(9), e1701497, 2017-09

    American Association for the Advancement of Science

Codes

  • NII Article ID (NAID)
    120006626420
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    2375-2548
  • Data Source
    IR 
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