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| [[Image:1by6.jpg|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1by6| PDB=1by6 | SCENE= }} | | {{STRUCTURE_1by6| PDB=1by6 | SCENE= }} |
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| '''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''
| | ===PEPTIDE OF HUMAN APOLIPOPROTEIN C-II=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_10903476}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 10903476 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_10903476}} |
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| ==About this Structure== | | ==About this Structure== |
| 1BY6 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA]. | | 1BY6 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA]. |
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| ==Reference== | | ==Reference== |
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| [[Category: Lipid association]] | | [[Category: Lipid association]] |
| [[Category: Lpl activation]] | | [[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 Mon Jun 30 19:54:17 2008'' |