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[[Image:1by6.jpg|left|200px]]<br /><applet load="1by6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1by6" />
'''PEPTIDE OF HUMAN APOLIPOPROTEIN C-II'''<br />


==Overview==
==Peptide of human apolipoprotein C-II==
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.
<StructureSection load='1by6' size='340' side='right'caption='[[1by6]]' scene=''>
 
== Structural highlights ==
==Disease==
<table><tr><td colspan='2'>[[1by6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY6 FirstGlance]. <br>
Known disease associated with this structure: Hyperlipoproteinemia, type Ib OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=608083 608083]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1by6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by6 OCA], [https://pdbe.org/1by6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by6 RCSB], [https://www.ebi.ac.uk/pdbsum/1by6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by6 ProSAT]</span></td></tr>
==About this Structure==
</table>
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].  
== Disease ==
 
[https://www.uniprot.org/uniprot/APOC2_HUMAN APOC2_HUMAN] Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:[https://omim.org/entry/207750 207750]. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.<ref>PMID:8323539</ref>
==Reference==
== Function ==
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10903476 10903476]
[https://www.uniprot.org/uniprot/APOC2_HUMAN APOC2_HUMAN] Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly.
[[Category: Single protein]]
== Evolutionary Conservation ==
[[Category: Cushley, R.J.]]
[[Image:Consurf_key_small.gif|200px|right]]
[[Category: Rozek, A.]]
Check<jmol>
[[Category: Sparrow, J.T.]]
  <jmolCheckbox>
[[Category: Storjohann, R.]]
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/by/1by6_consurf.spt"</scriptWhenChecked>
[[Category: amphipathic helix]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: apolipoprotein]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: lipid association]]
  </jmolCheckbox>
[[Category: lpl activation]]
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1by6 ConSurf].
 
<div style="clear:both"></div>
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:33:36 2008''
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cushley RJ]]
[[Category: Rozek A]]
[[Category: Sparrow JT]]
[[Category: Storjohann R]]

Latest revision as of 18:37, 13 March 2024

Peptide of human apolipoprotein C-IIPeptide of human apolipoprotein C-II

Structural highlights

1by6 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

APOC2_HUMAN Defects in APOC2 are the cause of hyperlipoproteinemia type 1B (HLPP1B) [MIM:207750. It is an autosomal recessive trait characterized by hypertriglyceridemia, xanthomas, and increased risk of pancreatitis and early atherosclerosis.[1]

Function

APOC2_HUMAN Component of the very low density lipoprotein (VLDL) fraction in plasma, and is an activator of several triacylglycerol lipases. The association of APOC2 with plasma chylomicrons, VLDL, and HDL is reversible, a function of the secretion and catabolism of triglyceride-rich lipoproteins, and changes rapidly.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

  1. ↑ Inadera H, Hibino A, Kobayashi J, Kanzaki T, Shirai K, Yukawa S, Saito Y, Yoshida S. A missense mutation (Trp 26-->Arg) in exon 3 of the apolipoprotein CII gene in a patient with apolipoprotein CII deficiency (apo CII-Wakayama). Biochem Biophys Res Commun. 1993 Jun 30;193(3):1174-83. PMID:8323539 doi:http://dx.doi.org/S0006-291X(83)71749-3
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