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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1995-1-19
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pubmed:abstractText |
Apolipoprotein-E (apo-E), a 34kDa blood plasma protein, plays a key role in directing cholesterol transport via its interaction with the low density lipoprotein (LDL) receptor. The amino-terminal domain of apo-E forms an unusually elongated four-helix bundle arranged such that key basic residues involved in LDL receptor binding form a cluster at the end of one of the helices. A common apo-E variant, apo-E2, corresponding to the single-site substitution Arg158-->Cys, displays minimal LDL receptor binding and is associated with significant changes in plasma cholesterol levels and increased risk of coronary heart disease. Surprisingly, the site of mutation in this variant is physically well removed (> 12A) from the cluster of LDL receptor binding residues.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0969-2126
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
713-8
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7994571-Apolipoprotein E2,
pubmed-meshheading:7994571-Apolipoproteins E,
pubmed-meshheading:7994571-Computer Simulation,
pubmed-meshheading:7994571-Crystallography,
pubmed-meshheading:7994571-Humans,
pubmed-meshheading:7994571-Models, Molecular,
pubmed-meshheading:7994571-Mutation,
pubmed-meshheading:7994571-Peptide Fragments,
pubmed-meshheading:7994571-Protein Conformation,
pubmed-meshheading:7994571-Receptors, LDL
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pubmed:year |
1994
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pubmed:articleTitle |
Salt bridge relay triggers defective LDL receptor binding by a mutant apolipoprotein.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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