Source:http://linkedlifedata.com/resource/pubmed/id/18428019
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2008-4-22
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pubmed:abstractText |
Atherosclerosis is a widespread disease caused by the deposition of lipids on arterial walls. Such lipid plaques in coronary arteries can be fatal. Although many factors related to diet, life-style, etc. contribute to the worsening of the ailment, the primary cause, the lipids in the circulatory system, come from a series of low-density lipoproteins. These lipoproteins are necessary for the transport of lipids to and from different organs. It would be valuable to medicine and the field of drug design if a more detailed understanding of the organization of lipid and protein in these molecules were available. Unfortunately because of heterogeneity in their size and lipid composition, all classes of the low-density serum lipoproteins appear to be not amenable to the most widely used method for obtaining detailed atomic data - X-ray crystallography. However there appears to be a recently identified homolog that is relatively homogeneous, and crystal structures have been obtained. Used as a molecular model, the homolog serves as a source of conformational information that might help to unravel the processes involved in the lipid loading of the low-density lipoproteins. The review attempts to give a brief summary of the structural biology of the serum low-density lipoproteins relative to the molecular model of lipovitellin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins B,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Egg Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/lipovitellin
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pubmed:status |
MEDLINE
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pubmed:issn |
1365-2060
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
253-67
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pubmed:meshHeading |
pubmed-meshheading:18428019-Animals,
pubmed-meshheading:18428019-Apolipoproteins B,
pubmed-meshheading:18428019-Atherosclerosis,
pubmed-meshheading:18428019-Carrier Proteins,
pubmed-meshheading:18428019-Crystallization,
pubmed-meshheading:18428019-Crystallography, X-Ray,
pubmed-meshheading:18428019-Egg Proteins,
pubmed-meshheading:18428019-Humans,
pubmed-meshheading:18428019-Lipoproteins, LDL,
pubmed-meshheading:18428019-Models, Molecular,
pubmed-meshheading:18428019-Protein Conformation
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pubmed:year |
2008
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pubmed:articleTitle |
The assembly of apoB-containing lipoproteins: a structural biology point of view.
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pubmed:affiliation |
Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, MN, USA. banas001@umn.edu
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pubmed:publicationType |
Journal Article,
Review
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