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-Structure paper
タイトル | Structure of the human dimeric ATM kinase. |
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ジャーナル・号・ページ | Cell Cycle, Vol. 15, Issue 8, Page 1117-1124, Year 2016 |
掲載日 | 2017年1月6日 |
著者 | Wilson C Y Lau / Yinyin Li / Zhe Liu / Yuanzhu Gao / Qinfen Zhang / Michael S Y Huen / |
PubMed 要旨 | DNA-double strand breaks activate the serine/threonine protein kinase ataxia-telangiectasia mutated (ATM) to initiate DNA damage signal transduction. This activation process involves ...DNA-double strand breaks activate the serine/threonine protein kinase ataxia-telangiectasia mutated (ATM) to initiate DNA damage signal transduction. This activation process involves autophosphorylation and dissociation of inert ATM dimers into monomers that are catalytically active. Using single-particle electron microscopy (EM), we determined the structure of dimeric ATM in its resting state. The EM map could accommodate the crystal structure of the N-terminal truncated mammalian target of rapamycin (mTOR), a closely related enzyme of the phosphatidylinositol 3-kinase-related protein kinase (PIKK) family, allowing for the localization of the N- and the C-terminal regions of ATM. In the dimeric structure, the actives sites are buried, restricting the access of the substrates to these sites. The unanticipated domain organization of ATM provides a basis for understanding its mechanism of inhibition. |
リンク | Cell Cycle / PubMed:27097373 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 28.0 Å |
構造データ | EMDB-6499: |
化合物 | ChemComp-ADP: ChemComp-MG: ChemComp-MGF: |
由来 |
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キーワード | TRANSFERASE / mTOR / PIKK |