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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site
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The solution structure of the Raf-1 cysteine-rich domain: A novel Ras and phospholipid binding site

机译:Raf-1富含半胱氨酸的结构域的溶液结构:一个新的Ras和磷脂结合位点

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摘要

The Raf-1 protein kinase is the best- characterized downstream effector of activated Ras. Interac- tion with Ras leads to Raf-1 activation and results in trans- duction of cell growth and differentiation signals. The details of Raf-1 activation are unclear, but our characterization of a second Ras-binding site in the cysteine-rich domain (CRD) and the involvement of both Ras-binding sites in effective Raf-1-mediated transformation provides insight into the mo- lecular aspects and consequences of Ras-Raf interactions.
机译:Raf-1蛋白激酶是活化Ras最具特征的下游效应子。与Ras的相互作用导致Raf-1活化,并导致细胞生长和分化信号的转导。 Raf-1激活的细节尚不清楚,但我们对富含半胱氨酸域(CRD)中第二个Ras结合位点的表征以及两个Ras结合位点在有效Raf-1介导的转化中的参与提供了深入的了解Ras-Raf相互作用的分子方面和后果。

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