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TitleThe crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 390, Page 780-785, Year 2009
Publish dateMar 27, 2009 (structure data deposition date)
AuthorsBakan, B. / Hamberg, M. / Larue, V. / Prange, T. / Marion, D. / Lascombe, M.B.
External linksBiochem. Biophys. Res. Commun. / PubMed:19836358
MethodsX-ray diffraction
Resolution1.8 Å
Structure data

PDB-3gsh:
Three-dimensional structure of a post translational modified barley LTP1
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-NA:
Unknown entry

ChemComp-TFA:
trifluoroacetic acid

ChemComp-ASY:
(12E)-10-oxooctadec-12-enoic acid

ChemComp-HOH:
WATER

Source
  • hordeum vulgare (barley)
KeywordsLIPID BINDING PROTEIN / LTP1 / POST-TRANSCRIPTIONAL MODIFICATION / OXYLIPIN / LIPID- BINDING / LIPOPROTEIN / TRANSPORT / Disulfide bond / Lipid-binding

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