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NMR structure of rALF-Pm3, an anti-lipopolysaccharide factor from shrimp: model of the possible lipid A-binding site Inra
Yang, Y.; Boze, H.; Chemardin, P.; Padilla, A.; Moulin, G.; Tassanakajon, A.; Pugnière, M.; Roquet, F.; Destoumieux-Garzon, D.; Gueguen, Y.; Bachère, E.; Aumelas, A..
The anti-lipopolysaccharide factor ALF-Pm3 is a 98-residue protein identified in hemocytes from the black tiger shrimp Penaeus monodon. It was expressed in Pichia pastoris from the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter as a folded and N-15 uniformly labeled rALF-Pm3 protein. Its 3D structure was established by NMR and consists of three alpha-helices packed against a four-stranded beta-sheet. The C-34-C-55 disulfide bond was shown to be essential for the structure stability. By using surface plasmon resonance, we demonstrated that rALF-Pm3 binds to LPS, lipid A and to OM(R)-174, a soluble analogue of lipid A. Biophysical studies of rALF-Pm3/LPS and rALF-Pm3/OM(R)-174 complexes indicated rather high molecular sized aggregates, which...
Tipo: Journal Article Palavras-chave: ANTI-LIPOPOLYSACCHARIDE FACTOR ; LIPOPOLYSACCHARIDE; LIPID A; NMR; STRUCTURE; SEPTIC SHOCK; SURFACE PLASMON RESONANCE ULTRACENTRIFUGATION.
Ano: 2009 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD201064bb8a78&uri=/notices/prodinra1/2010/09/
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