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…

Index: 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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Citation Number: 61

Abstract

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 ...