Modest effects of lipid modifications on the structure of caveolin-3
Ji-Hun Kim1, Dungeng Peng, Jonathan P Schlebach
1Department of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine , Nashville, Tennessee 37232, United States.
Abstract:
Caveolin-3 (Cav3) is an unconventional membrane protein that serves as a critical scaffolding hub in caveolae and is genetically linked to various muscle disorders. In this work, we report the expression, purification, and characterization of full-length human Cav3. To mimic the palmitoylation of endogenous Cav3, we developed a generally applicable approach to covalently attached thioalkyl chains at natively modified cysteine residues. Nuclear magnetic resonance measurements indicate that lipidation exerts only a modest and local effect on the Cav3 structure, with little impact on the structures of the N-terminal domain, the scaffolding domain, and the extreme C-terminus.
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