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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
23
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pubmed:dateCreated |
2010-6-9
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pubmed:abstractText |
Apolipoprotein (apo) A-V is a 343-residue, multidomain protein that plays an important role in regulation of plasma triglyceride homeostasis. Primary sequence analysis revealed a unique tetraproline sequence (Pro293-Pro296) near the carboxyl terminus of the protein. A peptide corresponding to the 48-residue segment beyond the tetraproline motif was generated from a recombinant apoA-V precursor wherein Pro295 was replaced by Met. Cyanogen bromide cleavage of the precursor protein, followed by negative affinity chromatography, yielded a purified peptide. Nondenaturing polyacrylamide gel electrophoresis verified that apoA-V(296-343) solubilizes phospholipid vesicles, forming a relatively heterogeneous population of reconstituted high-density lipoprotein with Stokes' diameters >17 nm. At the same time, apoA-V(296-343) failed to bind a spherical lipoprotein substrate in vitro. Far-UV circular dichroism spectroscopy revealed the peptide is unstructured in buffer yet adopts significant alpha-helical secondary structure in the presence of the lipid mimetic solvent trifluoroethanol (TFE; 50% v/v). Heteronuclear multidemensional NMR spectroscopy experiments were conducted with uniformly (15)N- and (15)N/(13)C-labeled peptide in 50% TFE. Peptide backbone assignment and secondary structure prediction using TALOS+ reveal the peptide adopts alpha-helix secondary structure from residues 309 to 334. In TFE, apoA-V(296-343) adopts an extended amphipathic alpha-helix, consistent with a role in lipoprotein binding as a component of full-length apoA-V.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-11577099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-11588264,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-12509990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-12899628,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-15234552,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-15528295,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-15591215,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-15774484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-15878877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-16200213,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-17326667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-17401142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-17495607,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-17985196,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-18056685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-18652480,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-19050314,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-19098282,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-19548092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-19825998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-3724517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-6048867,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-8422936,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-8520220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-8900168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20469899-9665727
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
49
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4821-6
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:20469899-Amino Acid Sequence,
pubmed-meshheading:20469899-Apolipoproteins A,
pubmed-meshheading:20469899-Circular Dichroism,
pubmed-meshheading:20469899-Lipid Bilayers,
pubmed-meshheading:20469899-Lipoproteins, HDL,
pubmed-meshheading:20469899-Methionine,
pubmed-meshheading:20469899-Molecular Sequence Data,
pubmed-meshheading:20469899-Mutagenesis, Site-Directed,
pubmed-meshheading:20469899-Mutation,
pubmed-meshheading:20469899-Peptide Fragments,
pubmed-meshheading:20469899-Proline,
pubmed-meshheading:20469899-Protein Binding,
pubmed-meshheading:20469899-Protein Conformation,
pubmed-meshheading:20469899-Protein Structure, Secondary
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pubmed:year |
2010
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pubmed:articleTitle |
The carboxyl-terminal segment of apolipoprotein A-V undergoes a lipid-induced conformational change.
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pubmed:affiliation |
Center for Prevention of Obesity, Cardiovascular Disease and Diabetes, Children's Hospital Oakland Research Institute, 5700 Martin Luther King Jr. Way, Oakland, California 94609, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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