The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins

B. Bakan (1) , M. Hamberg (2) , V. Larue (3) , T. Prangé (3) , D. Marion (1) , M.-B. Lascombe (3)

1 BIA - Unité de recherche sur les Biopolymères, Interactions Assemblages
2 Science for Life Laboratory, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, Stockholm, SE-17165 Sweden.
3 CiTCoM - UMR 8038 - Cibles Thérapeutiques et conception de médicaments

Domaines: Sciences du Vivant [q-bio]; Biochimie, Biologie Moléculaire; Biologie structurale [q-bio.BM]

B. Bakan, M. Hamberg, V. Larue, T. Prangé, D. Marion, et al.. The crystal structure of oxylipin-conjugated barley LTP1 highlights the unique plasticity of the hydrophobic cavity of these plant lipid-binding proteins. Biochemical and Biophysical Research Communications, 2009, 390 (3), pp.780-785. ⟨10.1016/j.bbrc.2009.10.049⟩. ⟨hal-02356184⟩