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| [[Image:1l6l.gif|left|200px]]<br />
| | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 1l6l was removed. |
| <applet load="1l6l" size="450" color="white" frame="true" align="right" spinBox="true"
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| caption="1l6l, resolution 2.3Å" />
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| '''Structures of Apolipoprotein A-II and a Lipid Surrogate Complex Provide Insights into Apolipoprotein-Lipid Interactions'''<br /> | |
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| ==Overview==
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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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| ==Disease==
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| Known diseases associated with this structure: Apolipoprotein A-II deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107670 107670]], Hypercholesterolemia, familial, modification of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107670 107670]]
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| ==About this Structure==
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| 1L6L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with BOG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L6L OCA].
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| ==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12269810 12269810]
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| [[Category: Homo sapiens]]
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| [[Category: Single protein]]
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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: BOG]]
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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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| ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:57:16 2007''
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For additional information see 2009, December: at Retractions and Fraud.
REMOVED: The PDB entry 1l6l was removed.
