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.

@article{Lerche1997BarleyLP,
  title={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.},
  author={Mathilde H. Lerche and Birthe B Kragelund and Lene M Bech and Flemming M. Poulsen},
  journal={Structure},
  year={1997},
  volume={5 2},
  pages={
          291-306
        }
}
BACKGROUND . 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. RESULTS . 1H and 13C nuclear magnetic resonance… CONTINUE READING
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