Journal
BIOCHEMISTRY
Volume 53, Issue 27, Pages 4320-4322Publisher
AMER CHEMICAL SOC
DOI: 10.1021/bi5005238
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Funding
- National Institutes of Health (NIH) [U54 GM094608, S10 RR025677-01]
- National Science Foundation [DBI-0922862]
- [RO1 GM106672]
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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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