Source:http://linkedlifedata.com/resource/pubmed/id/12801509
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2003-6-12
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pubmed:databankReference | |
pubmed:abstractText |
Plant nonspecific lipid transfer proteins (nsLTPs) are characterized by their ability to bind a broad range of hydrophobic ligands in vitro. Their biological function has not yet been elucidated, but they could play a major role in plant defense to physical and biological stress. An nsLTP was isolated from Amaranthus hypochondriacus seeds and purified by gel filtration and reversed-phase high-performance liquid chromatography techniques. The molecular mass of the protein as determined by mass spectrometry is 9747.29 Da. Data from amino acid sequence, circular dichroism and binding/displacement of a fluorescent lipid revealed that it belongs to the nsLTP1 family. The protein shows the alpha-helical secondary structure typical for plant nsLTPs 1 and shares 40 to 57% sequence identity with nsLTPs 1 from other plant species and 100% identity with an nsLTP1 from Amaranthus caudatus. A model structure of the protein in complex with stearate based on known structures of maize and rice nsLTPs 1 suggests a protein fold complexed with lipids closely related to that of maize nsLTP1.
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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/Antigens, Plant,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipids,
http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lipid transfer proteins, plant,
http://linkedlifedata.com/resource/pubmed/chemical/sterol carrier proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
415
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
24-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12801509-Amaranthus,
pubmed-meshheading:12801509-Amino Acid Sequence,
pubmed-meshheading:12801509-Antigens, Plant,
pubmed-meshheading:12801509-Carrier Proteins,
pubmed-meshheading:12801509-Chromatography, High Pressure Liquid,
pubmed-meshheading:12801509-Circular Dichroism,
pubmed-meshheading:12801509-Lipids,
pubmed-meshheading:12801509-Models, Molecular,
pubmed-meshheading:12801509-Molecular Sequence Data,
pubmed-meshheading:12801509-Molecular Weight,
pubmed-meshheading:12801509-Plant Proteins,
pubmed-meshheading:12801509-Protein Binding,
pubmed-meshheading:12801509-Protein Structure, Secondary,
pubmed-meshheading:12801509-Sequence Analysis, Protein,
pubmed-meshheading:12801509-Species Specificity,
pubmed-meshheading:12801509-Spectrometry, Mass, Matrix-Assisted Laser...
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pubmed:year |
2003
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pubmed:articleTitle |
Amino acid sequence, biochemical characterization, and comparative modeling of a nonspecific lipid transfer protein from Amaranthus hypochondriacus.
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pubmed:affiliation |
Departamento Sistemas Biológicos, UAM-X, 04960 México, D.F., Mexico.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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