期刊
BIOCHEMISTRY
卷 51, 期 1, 页码 90-99出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi201356v
关键词
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资金
- National Center for Research Resources (NCRR) [UL1 RR024153]
- University of Pittsburgh
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 alpha-helical structure, consistent with its commonly believed helical hairpin conformation. Intriguingly, in these same peptides, we observe a beta-stranded conformation for residues in the CSD, contrasting with earlier reports, which commonly do not reflect beta-structure. Our experimental data based on solid-state NMR, CD, and FTIR are found to be consistent with computational analyses of the secondary structure preference of the primary sequence. We discuss how our structural data of membrane binding Cav fragments may match certain general features of cholesterol-binding domains and could be consistent with the role for CSD in protein recognition and homo-oligomerization.
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