NMR Structure of Human Apolipoprotein C-II in the Presence of Sodium Dodecyl Sulfate
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- 作者：Christopher A. MacRaild ; Danny M. Hatters ; Geoffrey J. Howlett ; and Paul R. Gooley
- 刊名：Biochemistry
- 出版年：2001
- 出版时间：May 8, 2001
- 年：2001
- 卷：40
- 期：18
- 页码：5414 - 5421
- 全文大小：403K
- 年卷期：v.40,no.18(May 8, 2001)
- ISSN：1520-4995
文摘
The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presenceof SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques appliedto 15N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits theaggregation of apoC-II and induces a stable structure containing approximately 60% 
-helix as determinedby circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous andlargely disordered, with the rest of the protein forming a predominantly helical structure. Three regionsof helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints,with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shedlight on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.
-helix as determinedby circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous andlargely disordered, with the rest of the protein forming a predominantly helical structure. Three regionsof helical conformation, residues 16-36, 50-56, and 63-77, are well-defined by NMR-derived constraints,with the intervening regions showing more loosely defined helical conformation. The structure of apoC-II is compared to that determined for other apolipoproteins in a similar environment. Our results shedlight on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.