|
|
| (8 intermediate revisions by 2 users not shown) |
| Line 1: |
Line 1: |
| [[Image:2ou1.gif|left|200px]]
| | <span style='background-color: yellow;'>For additional information see '''2009, December:''' at [[Retractions and Fraud]].</span></br>REMOVED: The PDB entry 2ou1 was removed. |
| | |
| {{Structure
| |
| |PDB= 2ou1 |SIZE=350|CAPTION= <scene name='initialview01'>2ou1</scene>, resolution 2.0Å
| |
| |SITE=
| |
| |LIGAND=
| |
| |ACTIVITY=
| |
| |GENE=
| |
| |DOMAIN=
| |
| |RELATEDENTRY=[[1l6l|1L6L]]
| |
| |RESOURCES=<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://www.ebi.ac.uk/pdbsum/2ou1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ou1 RCSB]</span>
| |
| }}
| |
| | |
| '''Structures of apolipoprotein A-II and a lipid surrogate complex provide insights into apolipoprotein-lipid interactions''' | |
| | |
| | |
| ==Overview==
| |
| 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.
| |
| | |
| ==About this Structure==
| |
| 2OU1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry 1L6K. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OU1 OCA].
| |
| | |
| ==Reference==
| |
| 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://www.ncbi.nlm.nih.gov/pubmed/12269810 12269810]
| |
| [[Category: Homo sapiens]]
| |
| [[Category: Single protein]]
| |
| [[Category: Carson, M C.]]
| |
| [[Category: Hussain, M M.]]
| |
| [[Category: Kumar, M S.]]
| |
| [[Category: Murthy, H M.K.]]
| |
| [[Category: apolipoprotein]]
| |
| [[Category: apolipoprotein a-ii]]
| |
| [[Category: cholesterol metabolism x-ray diffraction]]
| |
| [[Category: helix]]
| |
| [[Category: high density lipoprotein]]
| |
| | |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:23:05 2008''
| |
For additional information see 2009, December: at Retractions and Fraud.
REMOVED: The PDB entry 2ou1 was removed.
