Linked Life Data

10672021

Source:http://linkedlifedata.com/resource/pubmed/id/10672021

Statements in which the resource exists.
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pubmed-article:10672021pubmed:abstractTextThe 3D solution structure of wheat nonspecific lipid transfer protein (ns-LTP) complexed with prostaglandin B2, a lipid with both vinyl and hydroxylated groups, has been determined by 1H 2D NMR. The global fold of the protein is close to the previously published structures of wheat, maize, barley and rice ns-LTPs. The ligand is almost completely embedded in the hydrophobic core of the protein. Structure comparisons of free and bound wheat ns-LTP reveal that the binding of prostaglandin B2 hardly affects the global fold of the protein. The structural data on this unusual complex are discussed and compared with other known ns-LTP lipid-complexes.lld:pubmed
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pubmed-article:10672021pubmed:articleTitleThe wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2.lld:pubmed
pubmed-article:10672021pubmed:affiliationCentre de Biophysique Moléculaire, UPR 4301 CNRS, Orléans, France; Université d'Orléans, France.lld:pubmed
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