1by6
From Proteopedia
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[[Image:1by6.jpg|left|200px]] | [[Image:1by6.jpg|left|200px]] | ||
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'''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II''' | '''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BY6 is a [[Single protein]] structure | + | 1BY6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Sparrow, J T.]] | [[Category: Sparrow, J T.]] | ||
[[Category: Storjohann, R.]] | [[Category: Storjohann, R.]] | ||
| - | [[Category: | + | [[Category: Amphipathic helix]] |
| - | [[Category: | + | [[Category: Apolipoprotein]] |
| - | [[Category: | + | [[Category: Lipid association]] |
| - | [[Category: | + | [[Category: Lpl activation]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:06:25 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:06, 2 May 2008
PEPTIDE OF HUMAN APOLIPOPROTEIN C-II
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.
About this Structure
1BY6 is a Single protein structure. 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 Page seeded by OCA on Fri May 2 12:06:25 2008
