Lipid modifications of a Ras peptide exhibit altered packing and mobility versus host membrane as detected by 2H solid-state NMR

…, CP Katzka, H Waldmann, K Arnold…

文献索引：Vogel, Alexander; Katzka, Catherine P.; Waldmann, Herbert; Arnold, Klaus; Brown, Michael F.; Huster, Daniel Journal of the American Chemical Society, 2005 , vol. 127, # 35 p. 12263 - 12272

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被引用次数: 61

摘要

The human N-ras protein binds to cellular membranes by insertion of two covalently bound posttranslational lipid modifications, which is crucial for its function in signal transduction and cell proliferation. Mutations in ras may lead to unregulated cell growth and eventually cancer, making it an important therapeutic target. Here we have investigated the molecular details of the membrane binding mechanism. A heptapeptide derived from the C-terminus ...