1i5j
From Proteopedia
(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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| - | [[Image:1i5j.gif|left|200px]]<br /> | + | [[Image:1i5j.gif|left|200px]]<br /><applet load="1i5j" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1i5j" size=" | + | |
caption="1i5j" /> | caption="1i5j" /> | ||
'''NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS'''<br /> | '''NMR STRUCTURE OF HUMAN APOLIPOPROTEIN C-II IN THE PRESENCE OF SDS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure and protein-detergent interactions of apolipoprotein C-II | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1I5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1I5J is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I5J OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Gooley, P | + | [[Category: Gooley, P R.]] |
| - | [[Category: Hatters, D | + | [[Category: Hatters, D M.]] |
| - | [[Category: Howlett, G | + | [[Category: Howlett, G J.]] |
| - | [[Category: MacRaild, C | + | [[Category: MacRaild, C A.]] |
[[Category: amphipathic alpha helix]] | [[Category: amphipathic alpha helix]] | ||
[[Category: protein-lipid interaction]] | [[Category: protein-lipid interaction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:08:12 2008'' |
Revision as of 11:08, 21 February 2008
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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
Page seeded by OCA on Thu Feb 21 13:08:12 2008
