1i5j
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(New page: 200px<br /> <applet load="1i5j" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i5j" /> '''NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II ...)
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Revision as of 15:20, 12 November 2007
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NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS
Contents |
Overview
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.
Disease
Known disease associated with this structure: Hyperlipoproteinemia, type Ib OMIM:[608083]
About this Structure
1I5J is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
NMR structure of human apolipoprotein C-II in the presence of sodium dodecyl sulfate., MacRaild CA, Hatters DM, Howlett GJ, Gooley PR, Biochemistry. 2001 May 8;40(18):5414-21. PMID:11331005
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