1I5J

NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS

1I5J の概要

• エントリーDOI: 10.2210/pdb1i5j/pdb
• 分子名称: APOLIPOPROTEIN CII (1 entity in total)
• 機能のキーワード: protein-lipid interaction, amphipathic alpha helix, lipid transport
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8921.86

構造登録者

MacRaild, C.A.,Hatters, D.M.,Howlett, G.J.,Gooley, P.R. (登録日: 2001-02-27, 公開日: 2001-05-16, 最終更新日: 2024-05-22)

主引用文献

MacRaild, C.A.,Hatters, D.M.,Howlett, G.J.,Gooley, P.R.
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate.
Biochemistry, 40:5414-5421, 2001

PubMed Abstract: The structure and protein-detergent interactions of apolipoprotein C-II (apoC-II) in the presence of SDS micelles have been investigated using circular dichroism and heteronuclear NMR techniques applied to (15)N-labeled protein. Micellar SDS, a commonly used mimetic of the lipoprotein surface, inhibits the aggregation of apoC-II and induces a stable structure containing approximately 60% alpha-helix as determined by circular dichroism. NMR reveals the first 12 residues of apoC-II to be structurally heterogeneous and largely disordered, with the rest of the protein forming a predominantly helical structure. Three regions of 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 shed light on the lipid interactions of apoC-II and its mechanism of lipoprotein lipase activation.

PubMed: 11331005
DOI: 10.1021/bi002821m

実験手法

SOLUTION NMR