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Updated: Mar 30, 2026

X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050
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X-Ray Crystallography to Study the Oligomeric State Transition of the Thermotoga maritima M42 Aminopeptidase TmPep1050

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ERMタンパク質モエシンの構造は,拡張されたアクチン結合尾領域によってマスクされたFERMドメインの折り畳みを明らかにします

M A Pearson1, D Reczek, A Bretscher

  • 1Department of Molecular Biology and Genetics, Cornell University, Ithaca, New York 14853, USA.

Cell
|June 10, 2000
PubMed
まとめ

エズリン-ラジシン-モエシン (ERM) タンパク質ファミリーは細胞構造を調節する. 彼らの休眠状態は,FERMとテールドメインの相互作用を含む新しい活性化メカニズムを明らかにし,細胞シグナル伝達とメルリン調節の洞察を提供します.

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