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| - | | + | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 2ou1 was removed. |
| - | ==Structures of apolipoprotein A-II and a lipid surrogate complex provide insights into apolipoprotein-lipid interactions==
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| - | <StructureSection load='2ou1' size='340' side='right' caption='[[2ou1]], [[Resolution|resolution]] 2.00Å' scene=''> | + | |
| - | == Structural highlights ==
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| - | <table><tr><td colspan='2'>[[2ou1]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1l6k 1l6k]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OU1 FirstGlance]. <br>
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| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1l6l|1l6l]]</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=2ou1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ou1 OCA], [http://pdbe.org/2ou1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ou1 RCSB], [http://www.ebi.ac.uk/pdbsum/2ou1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ou1 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/ou/2ou1_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=2ou1 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 2ou1" 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 C]]
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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 x-ray diffraction]]
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| - | [[Category: Helix]]
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| - | [[Category: High density lipoprotein]]
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| - | [[Category: Lipid binding protein]]
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