A Photoactivatable Prenylated Cysteine Designed to Study Isoprenoid Recognition

• Published in: Journal of the American Chemical Society Vol. 123; no. 19; pp. 4373 - 4381
• Main Authors: Kale, Tamara A, Raab, Conrad, Yu, Nathan, Dean, Dennis C, Distefano, Mark D
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 16.05.2001; Amer Chemical Soc
• Subjects: Binding, Competitive; cdc42 GTP-Binding Protein - chemistry; Chemistry; Chemistry, Multidisciplinary; Cross-Linking Reagents; Cysteine - analogs & derivatives; Cysteine - chemical synthesis; Escherichia coli - chemistry; Indicators and Reagents; Isotope Labeling; Molecular Mimicry; Photochemistry; Photolysis; Physical Sciences; Polyisoprenyl Phosphates - chemistry; Precipitin Tests; Protein Prenylation; Science & Technology; Spectrophotometry, Ultraviolet; Sulfur Radioisotopes; REGIOSELECTIVE ISOPRENYLATION; DISSOCIATION INHIBITORS; YEAST PROTEIN FARNESYLTRANSFERASE; BETA-GAMMA COMPLEX; RAS; ANALOGS; RHO; FARNESYL; RECEPTOR; BINDING

Protein prenylation, involving the alkylation of a specific C-terminal cysteine with a C15 or C20 isoprenoid unit, is an essential posttranslational modification required by most GTP-binding proteins for normal biological activity. Despite the ubiquitous nature of this modification and numerous effo...