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rdf:type |
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lifeskim:mentions |
umls-concept:C0004755,
umls-concept:C0005456,
umls-concept:C0009951,
umls-concept:C0023688,
umls-concept:C0030239,
umls-concept:C0424576,
umls-concept:C0598629,
umls-concept:C0678594,
umls-concept:C1095831,
umls-concept:C1180347,
umls-concept:C2349186
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pubmed:issue |
2
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pubmed:dateCreated |
1997-6-3
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pubmed:abstractText |
. Plant nonspecific lipid-transfer proteins (nsLTPs) bind a variety of very different lipids in vitro, including phospholipids, glycolipids, fatty acids and acyl coenzyme As. In this study we have determined the structure of a nsLTP complexed with palmitoyl coenzyme A (PCoA) in order to further our understanding of the structural mechanism of the broad specificity of these proteins and its relation to the function of nsLTPs in vivo.
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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 |
Feb
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pubmed:issn |
0969-2126
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
5
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
291-306
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:9032083-Amino Acid Sequence,
pubmed-meshheading:9032083-Animals,
pubmed-meshheading:9032083-Antigens, Plant,
pubmed-meshheading:9032083-Binding Sites,
pubmed-meshheading:9032083-Carrier Proteins,
pubmed-meshheading:9032083-Chemistry, Physical,
pubmed-meshheading:9032083-Fatty Acid-Binding Proteins,
pubmed-meshheading:9032083-Hordeum,
pubmed-meshheading:9032083-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9032083-Models, Molecular,
pubmed-meshheading:9032083-Molecular Sequence Data,
pubmed-meshheading:9032083-Myelin P2 Protein,
pubmed-meshheading:9032083-Neoplasm Proteins,
pubmed-meshheading:9032083-Palmitoyl Coenzyme A,
pubmed-meshheading:9032083-Physicochemical Phenomena,
pubmed-meshheading:9032083-Plant Proteins,
pubmed-meshheading:9032083-Protein Binding,
pubmed-meshheading:9032083-Protein Conformation
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pubmed:year |
1997
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pubmed:articleTitle |
Barley lipid-transfer protein complexed with palmitoyl CoA: the structure reveals a hydrophobic binding site that can expand to fit both large and small lipid-like ligands.
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pubmed:affiliation |
Carlsberg Laboratorium, Kemisk Afdeling, Gamle Carlsberg Vej 10, DK-2500 Valby, Copenhagen, Denmark.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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