Journal
BIOPHYSICAL JOURNAL
Volume 109, Issue 8, Pages 1686-1688Publisher
CELL PRESS
DOI: 10.1016/j.bpj.2015.08.030
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Funding
- NIGMS NIH HHS [R01-GM093258-01A1, R01 GM093258] Funding Source: Medline
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Caveolin-1 is an integral membrane protein that is the primary component of cell membrane invaginations called caveolae. While caveolin-1 is known to participate in a myriad of vital cellular processes, structural data on caveolin-1 of any kind is severely limited. In order to rectify this dearth, secondary structure analysis of a functional construct of caveolin-1, containing the intact C-terminal domain, was performed using NMR spectroscopy in lyso-myristoylphosphatidylglycerol micelles. Complete backbone assignments of caveolin-1 (residues 62-178) were made, and it was determined that residues 62-79 were dynamic; residues 89-107,111-128, and 132-175 were helical; and residues 80-88, 108-110, and 129-131 represent unstructured breaks between the helices.
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