2ou1
From Proteopedia
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[[Image:2ou1.gif|left|200px]] | [[Image:2ou1.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_2ou1| PDB=2ou1 | SCENE= }} | |
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'''Structures of apolipoprotein A-II and a lipid surrogate complex provide insights into apolipoprotein-lipid interactions''' | '''Structures of apolipoprotein A-II and a lipid surrogate complex provide insights into apolipoprotein-lipid interactions''' | ||
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==About this Structure== | ==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 | + | 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 [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]. |
==Reference== | ==Reference== | ||
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[[Category: Kumar, M S.]] | [[Category: Kumar, M S.]] | ||
[[Category: Murthy, H M.K.]] | [[Category: Murthy, H M.K.]] | ||
| - | [[Category: | + | [[Category: Apolipoprotein]] |
| - | [[Category: | + | [[Category: Apolipoprotein a-ii]] |
| - | [[Category: | + | [[Category: Cholesterol metabolism x-ray diffraction]] |
| - | [[Category: | + | [[Category: Helix]] |
| - | [[Category: | + | [[Category: High density lipoprotein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 11:39:13 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:39, 4 May 2008
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 Homo sapiens. This structure supersedes the now removed PDB entry 1l6k. Full crystallographic information is available from 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:12269810 Page seeded by OCA on Sun May 4 11:39:13 2008
