4 years ago

Mechanistic basis for the recognition of laminin-511 by {alpha}6{beta}1 integrin

Kiyotoshi Sekiguchi, Erika Yamashita, Junichi Takagi, Takao Arimori, Mamoru Takizawa, Yu Kitago, Yukimasa Taniguchi

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 chain (-tail)—are required for integrin binding, but it remains unclear how the -tail contributes to the binding. We determined the crystal structure of the integrin binding fragment of laminin-511, showing that the -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 1-tail apposed to the metal ion–dependent adhesion site (MIDAS) of integrin β1. These findings are consistent with a model in which the -tail coordinates the metal ion in the MIDAS through its Glu residue.

Publisher URL: http://advances.sciencemag.org/cgi/content/short/3/9/e1701497

DOI: 10.1126/sciadv.1701497

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