Structural characterization of the caveolin scaffolding domain in association with cholesterol-rich membranes.

ABSTRACT: Members of the caveolin protein family are implicated in the formation of caveolae and play important roles in a number of signaling pathways and in the regulation of various proteins. We employ complementary spectroscopic methods to study the structure of the caveolin scaffolding domain (CSD) in caveolin-1 fragments, while bound to cholesterol-rich membranes. This key domain is thought to be involved in multiple critical functions that include protein recognition, oligomerization, and cholesterol binding. In our membrane-bound peptides, residues within the flanking intramembrane domain (IMD) are found to adopt an α-helical structure, consistent with its commonly believed helical hairpin conformation. Intriguingly, in these same peptides, we observe a β-stranded conformation for residues i

SUBMITTER: Hoop CL 

PROVIDER: S-EPMC3290515 | biostudies-literature | 2012 Jan

REPOSITORIES: biostudies-literature