par Garcia-Pino, Abel 
;Buts, Lieven;Wyns, Lode;Imberty, Anne;Loris, Remy
Référence Plant physiology, 144, 4, page (1733-1741)
Publication Publié, 2007-08
;Buts, Lieven;Wyns, Lode;Imberty, Anne;Loris, RemyRéférence Plant physiology, 144, 4, page (1733-1741)
Publication Publié, 2007-08
Article révisé par les pairs
| Résumé : | The crystal structure of Pterocarpus angolensis seed lectin is presented in complex with a series of high mannose (Man) oligosaccharides ranging from Man-5 to Man-9. Despite that several of the nine Man residues of Man-9 have the potential to bind in the monosaccharide-binding site, all oligomannoses are bound in the same unique way, employing the tetrasaccharide sequence Manalpha(1-2)Manalpha(1-6)[Manalpha(1-3)]Manalpha(1-. Isothermal titration calorimetry titration experiments using Man-5, Man-9, and the Man-9-containing glycoprotein soybean (Glycine max) agglutinin as ligands confirm the monovalence of Man-9 and show a 4-times higher affinity for Man-9 when it is presented to P. angolensis seed lectin in a glycoprotein context. |
