Title | How a plant lectin recognizes high mannose oligosaccharides. |
Publication Type | Journal Article |
Year of Publication | 2007 |
Authors | Garcia-Pino, A., L. Buts, L. Wyns, A. Imberty, and R. Loris |
Journal | Plant Physiol |
Volume | 144 |
Issue | 4 |
Pagination | 1733-41 |
Date Published | 2007 Aug |
Type of Article | lectins |
ISSN | 0032-0889 |
Keywords | Binding Sites, Crystallography, X-Ray, Ligands, Mannose, Mannose-Binding Lectins, Molecular Conformation, Oligosaccharides, Pterocarpus, Seeds, Thermodynamics |
Abstract | 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. |
DOI | 10.1104/pp.107.100867 |
Alternate Journal | Plant Physiol. |
PubMed ID | 17556509 |
PubMed Central ID | PMC1949895 |
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