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''' | + | {{Structure |
| + | |PDB= 1by6 |SIZE=350|CAPTION= <scene name='initialview01'>1by6</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BY6 is a [ | + | 1BY6 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10903476 10903476] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cushley, R J.]] | [[Category: Cushley, R J.]] | ||
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[[Category: lpl activation]] | [[Category: lpl activation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:22 2008'' |
Revision as of 08:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Thu Mar 20 10:17:22 2008
