Accueil > Publications > Recherche par années > Années 2000 > 2006

Da Silva, P ; Landon, C ; Beltoise, R ; Ponchet, M ; Vovelle, F

Accessibility of tobacco lipid transfer protein cavity revealed by N-15 NMR relaxation studies and molecular dynamics simulations

Proteins-Structure Function and Bioinformatics 64 (1) 124-132

par Administrateur - publié le

Abstract :

Plant LTP1 are small helical proteins stabilized by four disulfide bridges and are characterized by the presence of an internal cavity, in which various hydrophobic ligands can be inserted. Recently, we have determined the solution structure of the recombinant tobacco LTP1_1. Unexpectedly, despite a global fold very similar to the structures already known for cereal seed LTP1, its binding properties are different : Tobacco LTP1_1 is able to bind only one monoacylated lipid, whereas cereal LTP1 can bind either one or two. The 3D structure of tobacco LTP1_1 revealed the presence of a hydrophobic cluster, not observed on cereal LTP1 structures, which may hinder one of the two entrances of the cavity defined for wheat LTP1.