1by6
From Proteopedia
(New page: 200px<br /> <applet load="1by6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by6" /> '''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''<br ...) |
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'''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''<br /> | '''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1BY6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: lpl activation]] | [[Category: lpl activation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:36 2008'' |
Revision as of 13:33, 15 February 2008
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PEPTIDE OF HUMAN APOLIPOPROTEIN C-II
Contents |
Overview
We have studied the three-dimensional structure of a biologically active, peptide of apolipoprotein C-II (apoC-II) in the presence of lipid mimetics, by CD and NMR spectroscopy. This peptide, corresponding to residues 44-79, of apoC-II, has been shown to reverse the symptoms of genetic apoC-II, deficiency in a human subject. A comparison of alpha-proton secondary, shifts and CD spectroscopic data indicates that the structure of, apoC-II(44-79) is similar in the presence of dodecylphosphocholine and, sodium dodecyl sulfate. The three-dimensional structure of apoC-II(44-79), in the presence of sodium dodecyl sulfate, determined by relaxation matrix, calculations, contains two amphipathic helical domains formed by residues, 50-58 and 67-75, separated by a non-helical linker centered at Tyr63. The, C-terminal helix is terminated by a loop formed by residues 76-79. The, C-terminal helix is better defined and has a larger hydrophobic face than, the N-terminal helix, which leads us to propose that the C-terminal helix, together with the non-helical Ile66 constitute the primary lipid binding, domain of apoC-II(44-79). Based on our structure we suggest a new, mechanism of lipoprotein lipase activation in which both helices of, apoC-II(44-79) remain lipid bound, while the seven-residue interhelical, linker extends away from the lipid surface in order to project Tyr63 into, the apoC-II binding site of lipoprotein lipase.
Disease
Known disease associated with this structure: Hyperlipoproteinemia, type Ib OMIM:[608083]
About this Structure
1BY6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of a biologically active fragment of human serum apolipoprotein C-II in the presence of sodium dodecyl sulfate and dodecylphosphocholine., Storjohann R, Rozek A, Sparrow JT, Cushley RJ, Biochim Biophys Acta. 2000 Jul 19;1486(2-3):253-64. PMID:10903476
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