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Refined solution structure of a liganded type 2 wheat nonspecific lipid transfer protein Inra
Pons, J.L.; de Lamotte, F.; Gautier, M.F.; Delsuc, M.A..
The refined structure of a wheat type 2 nonspecific lipid transfer protein (ns-LTP2) liganded withl-α-palmitoylphosphatidylglycerol has been determined by NMR. The 15N-labeled protein was produced in Pichia pastoris. Physicochemical conditions and ligandation were intensively screened to obtain the best NMR spectra quality. This ns-LTP2 is a 67-residue globular protein with a diameter of about 30 Å. The structure is composed of five helices forming a right superhelix. The protein presents an inner cavity, which has been measured at 341 Å3. All of the helices display hydrophobic side chains oriented toward the cavity. The phospholipid is found in this cavity. Its fatty acid chain is completely inserted in the protein, the l-α-palmitoylphosphatidylglycerol...
Tipo: Journal Article Palavras-chave: PROTEINE TRANSFERT DE LIPIDE; BIOCHIMIE STRUCTURALE; SPECTROSCOPIE RMN; TECHNIQUE ANALYTIQUE; PICHIA PASTORIS; STRUCTURE TRIDIMENSIONNELLE; PLANTE; SEQUENCE NUCLEOTIDIQUE; PHOSPHOLIPIDE; LIAISON.
Ano: 2003 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PUB0400023062101609&uri=/notices/prodinra1/2010/11/
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Single-chain variable fragments antibody specific toCorynespora cassiicola toxin, cassiicolin, reduces necrotic lesion formation in Hevea brasiliensis Inra
Sunderasan, E.; Kadir, R.A.; Pujade-Renaud, V.; de Lamotte, F.; Yeang, H.Y.; Nathan, S..
Corynespora leaf disease poses a serious threat to rubber cultivation because infected leaves develop necrotic lesions and abscise, leaving the tree unproductive. The destructiveness of Corynespora cassiicola has been largely attributed to cassiicolin, a protein toxin secreted by the fungus. Recombinant antibody technology offers hope to curtail the disease whereby single-chain variable fragments (scFv) specific to cassiicolin could bind and deactivate the toxin in genetically modified rubber trees that harbour the antibody gene. A scFv phage library was constructed from heavy and light variable chains of IgG from cassiicolin immunized Balb/C mice spleen. Biopanning of the phage library yielded a scFv clone with high specificity to cassiicolin. The...
Tipo: Journal Article Palavras-chave: CLONE; OLIGONUCLEOTIDE CORYNESPORA CASSIICOLA; CASSIICOLIN; ANTI-CASSIICOLIN SCFV; DETACHED HEVEA LEAF BIOASSAY.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2009c497e060&uri=/notices/prodinra1/2010/03/
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