The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2

Eur J Biochem. 2000 Feb;267(4):1117-24. doi: 10.1046/j.1432-1327.2000.01109.x.

Abstract

The 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • Fatty Acids / metabolism
  • Ligands
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Prostaglandins B / chemistry
  • Prostaglandins B / metabolism*
  • Protein Binding
  • Protein Conformation
  • Protein Folding
  • Solutions
  • Triticum / chemistry*

Substances

  • Carrier Proteins
  • Fatty Acids
  • Ligands
  • Plant Proteins
  • Prostaglandins B
  • Solutions
  • sterol carrier proteins
  • prostaglandin B2