title: Modest effects of lipid modifications on the structure of caveolin-3.
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.
authors: Department of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine , Nashville, Tennessee 37232, United States.
authors: Ji-Hun
authors: JH
authors: Kim
authors: Dungeng
authors: D
authors: Peng
authors: Jonathan P
authors: JP
authors: Schlebach
authors: Arina
authors: A
authors: Hadziselimovic
authors: Charles R
authors: CR
authors: Sanders
mesh_terms: D051244:Caveolin 3 / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D054878:Lipoylation; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics
chemical_list: D051244:Caveolin 3; D011994:Recombinant Proteins