| pubmed-article:16452169 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16452169 | lifeskim:mentions | umls-concept:C0007222 | lld:lifeskim |
| pubmed-article:16452169 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:16452169 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:16452169 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:16452169 | lifeskim:mentions | umls-concept:C1677784 | lld:lifeskim |
| pubmed-article:16452169 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:16452169 | pubmed:dateCreated | 2006-2-15 | lld:pubmed |
| pubmed-article:16452169 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16452169 | pubmed:abstractText | Despite three decades of extensive studies on human apolipoprotein A-I (apoA-I), the major protein component in high-density lipoproteins, the molecular basis for its antiatherogenic function is elusive, in part because of lack of a structure of the full-length protein. We describe here the crystal structure of lipid-free apoA-I at 2.4 A. The structure shows that apoA-I is comprised of an N-terminal four-helix bundle and two C-terminal helices. The N-terminal domain plays a prominent role in maintaining its lipid-free conformation, indicating that mutants with truncations in this region form inadequate models for explaining functional properties of apoA-I. A model for transformation of the lipid-free conformation to the high-density lipoprotein-bound form follows from an analysis of solvent-accessible hydrophobic patches on the surface of the structure and their proximity to the hydrophobic core of the four-helix bundle. The crystal structure of human apoA-I displays a hitherto-unobserved array of positively and negatively charged areas on the surface. Positioning of the charged surface patches relative to hydrophobic regions near the C terminus of the protein offers insights into its interaction with cell-surface components of the reverse cholesterol transport pathway and antiatherogenic properties of this protein. This structure provides a much-needed structural template for exploration of molecular mechanisms by which human apoA-I ameliorates atherosclerosis and inflammatory diseases. | lld:pubmed |
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| pubmed-article:16452169 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16452169 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16452169 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16452169 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16452169 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:16452169 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:16452169 | pubmed:author | pubmed-author:Anantharamaia... | lld:pubmed |
| pubmed-article:16452169 | pubmed:author | pubmed-author:HussainM... | lld:pubmed |
| pubmed-article:16452169 | pubmed:author | pubmed-author:MurthyH M... | lld:pubmed |
| pubmed-article:16452169 | pubmed:author | pubmed-author:MishraVinod... | lld:pubmed |
| pubmed-article:16452169 | pubmed:author | pubmed-author:AjeesA... | lld:pubmed |
| pubmed-article:16452169 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16452169 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:16452169 | pubmed:volume | 103 | lld:pubmed |
| pubmed-article:16452169 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16452169 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16452169 | pubmed:pagination | 2126-31 | lld:pubmed |
| pubmed-article:16452169 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
| pubmed-article:16452169 | pubmed:meshHeading | pubmed-meshheading:16452169... | lld:pubmed |
| pubmed-article:16452169 | pubmed:meshHeading | pubmed-meshheading:16452169... | lld:pubmed |
| pubmed-article:16452169 | pubmed:meshHeading | pubmed-meshheading:16452169... | lld:pubmed |
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| pubmed-article:16452169 | pubmed:meshHeading | pubmed-meshheading:16452169... | lld:pubmed |
| pubmed-article:16452169 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16452169 | pubmed:articleTitle | Crystal structure of human apolipoprotein A-I: insights into its protective effect against cardiovascular diseases. | lld:pubmed |
| pubmed-article:16452169 | pubmed:affiliation | Center for Biophysical Sciences and Engineering and Atherosclerosis Research Unit and Department of Medicine, University of Alabama, 1530 3rd Avenue South, Birmingham, AL 35294, USA. | lld:pubmed |
| pubmed-article:16452169 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16452169 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:16452169 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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