'''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===
==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.
The line below this paragraph, {{ABSTRACT_PUBMED_12269810}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 12269810 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_12269810}}
==About this Structure==
==About this Structure==
Line 31:
Line 35:
[[Category: Helix]]
[[Category: Helix]]
[[Category: High density lipoprotein]]
[[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 Tue Jul 29 00:09:37 2008''
Revision as of 21:09, 28 July 2008
This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.
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
