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| <table cellpadding='5'><tr><td style='background-color: yellow;border:2px solid black;font-size:150%;'> | | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 1l6l was removed. |
| WARNING: This structure was flagged as problematic. For additional information see '''2009, December:''' at [[Retractions and Fraud]].</td></tr></table>
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| ==Structures of Apolipoprotein A-II and a Lipid Surrogate Complex Provide Insights into Apolipoprotein-Lipid Interactions==
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| <StructureSection load='1l6l' size='340' side='right' caption='[[1l6l]], [[Resolution|resolution]] 2.30Å' scene=''>
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| == Structural highlights ==
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| <table><tr><td colspan='2'>[[1l6l]] is a 32 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L6L FirstGlance]. <br>
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| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr>
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| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l6k|1l6k]]</td></tr>
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| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l6l OCA], [http://pdbe.org/1l6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l6l RCSB], [http://www.ebi.ac.uk/pdbsum/1l6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l6l ProSAT]</span></td></tr>
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| </table>
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| == Function ==
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| [[http://www.uniprot.org/uniprot/APOA2_HUMAN APOA2_HUMAN]] May stabilize HDL (high density lipoprotein) structure by its association with lipids, and affect the HDL metabolism.
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| == Evolutionary Conservation ==
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| [[Image:Consurf_key_small.gif|200px|right]]
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| Check<jmol>
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| <jmolCheckbox>
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| <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l6/1l6l_consurf.spt"</scriptWhenChecked>
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| <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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| <text>to colour the structure by Evolutionary Conservation</text>
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| </jmolCheckbox>
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| </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=1l6l ConSurf].
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| <div style="clear:both"></div>
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Apolipoproteins A-I and A-II form the major protein constituents of high-density lipid particles (HDL), the concentration of which is inversely correlated with the frequency of heart disease in humans. Although the physiological role of apolipoprotein A-II is unclear, evidence for its involvement in free fatty acid metabolism in mice has recently been obtained. Currently, the best characterized activity of apolipoprotein A-II is its potent antagonism of the anti-atherogenic and anti-inflammatory activities of apolipoprotein A-I, probably due to its competition with the latter for lipid acyl side chains in HDL. Many interactions of apolipoprotein A-I with enzymes and proteins involved in reverse cholesterol transport and HDL maturation are mediated by lipid-bound protein. The structural bases of interaction with lipids are expected to be common to exchangeable apolipoproteins and attributable to amphipathic alpha-helices present in each of them. Thus, characterization of apolipoprotein-lipid interactions in any apolipoprotein is likely to provide information that is applicable to the entire class. We report structures of human apolipoprotein A-II and its complex with beta-octyl glucoside, a widely used lipid surrogate. The former shows that disulfide-linked dimers of apolipoprotein A-II form amphipathic alpha-helices which aggregate into tetramers. Dramatic changes, observed in the presence of beta-octyl glucoside, might provide clues to the structural basis for its antagonism of apolipoprotein A-I. Additionally, excursions of individual molecules of apolipoprotein A-II from a common helical architecture in both structures indicate that lipid-bound apolipoproteins are likely to have an ensemble of related conformations. These structures provide the first experimental paradigm for description of apolipoprotein-lipid interactions at the atomic level.
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| Structures of apolipoprotein A-II and a lipid-surrogate complex provide insights into apolipoprotein-lipid interactions.,Kumar MS, Carson M, Hussain MM, Murthy HM Biochemistry. 2002 Oct 1;41(39):11681-91. PMID:12269810<ref>PMID:12269810</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1l6l" style="background-color:#fffaf0;"></div>
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| ==See Also==
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| *[[Retractions and Fraud|Retractions and Fraud]]
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| == References ==
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| <references/>
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| __TOC__
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| </StructureSection>
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| [[Category: Homo sapiens]]
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| [[Category: Carson, M]]
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| [[Category: Hussain, M M]]
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| [[Category: Kumar, M S]]
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| [[Category: Murthy, H M.K]]
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| [[Category: Apolipoprotein]]
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| [[Category: Apolipoprotein a-ii]]
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| [[Category: Cholesterol metabolism]]
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| [[Category: Helix]]
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| [[Category: High density lipid]]
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| [[Category: Lipid transport]]
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For additional information see 2009, December: at Retractions and Fraud.
REMOVED: The PDB entry 1l6l was removed.