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Key interactions in integrin ectodomain responsible for global conformational change detected by elastic network normal-mode analysis

Matsumoto, Atsushi; Kamata, Tetsuji*; Takagi, Junichi*; Iwasaki, Kenji*; Yura, Kei

Protein is activated, but the activation mechanism and generality of the conformational change remain to be elucidated. We performed normal mode analysis of the elastic network model on integrin $$alpha$$$$_{V}$$$$beta$$$$_{3}$$ ectodomain in the bent form and identified key residues which were influential on molecular motions. Iterative normal mode calculations demonstrated that the specific non-bonded interactions involving the key residues work as a snap to keep integrin in the bent form. The importance of the key residues for the conformational change was further verified by mutation experiments. Conservation pattern of amino acid residues among integrin family showed that the characteristic pattern of residues seen around these key residues is found in the limited groups of integrin $$beta$$ chains.

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Category:Biophysics

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