High impact information on ltp-BR1

• We have found and characterized a novel post-translational modification of the barley nonspecific lipid transfer protein, LTP1 [1].
• The p48h-10-encoded protein shares some common characteristics of plant nonspecific lipid transfer proteins (low molecular weight, the secretion signal peptide, eight conserved cysteine residues, and a basic protein), although no significant protein sequence homology is found between p48-10 and other plant nonspecific lipid transfer proteins [2].
• Solution structure of barley lipid transfer protein complexed with palmitate. Two different binding modes of palmitate in the homologous maize and barley nonspecific lipid transfer proteins [3].
• In order to investigate the nature of genes expressed in leaf epidermal cells of higher plants, we have identified the nucleotide sequence of a cDNA designated ltp 7a2b encoding a novel nonspecific lipid transfer protein of barley (Hordeum vulgare L. cv. Gerbel) [4].
• In bLTP, the residues analogous to those in maize nsLTP that constitute the palmitate binding site are forming a similar hydrophobic cavity and a potential acyl group binding site [5].

Anatomical context of ltp-BR1

• Several small plant proteins with the ability to mediate transfer of radiolabeled phospholipids in vitro from liposomal donor membranes to mitochondrial and chloroplast acceptor membranes have been isolated, and a protein with this ability, the nonspecific lipid transfer protein (nsLTP) isolated from barley seeds (bLTP), has been studied here [5].

Associations of ltp-BR1 with chemical compounds

• Structure comparisons of free and bound wheat ns-LTP reveal that the binding of prostaglandin B2 hardly affects the global fold of the protein [6].

Analytical, diagnostic and therapeutic context of ltp-BR1

• Here we describe the functional dissection of the barley nonspecific lipid transfer protein gene promoter, HvLTP2 [7].

References