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How a plant lectin recognizes high mannose oligosaccharides

Publication Type:

Journal Article

Authors:

Garcia-Pino,A.; Buts,L.; Wyns,L.; Imberty,A.; Loris,R.

Source:

Volume 144, Issue 4, p.1733 - 1741 (2007)

URL:

PM:17556509

Keywords:

Binding Sites; Crystallography; X-Ray; Ligands; Mannose; metabolism; Mannose-Binding Lectins; chemistry; 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

Notes:

DA - 20070809
IS - 0032-0889 (Print)
LA - eng
PT - Journal Article
PT - Research Support, Non-U.S. Gov't
RN - 0 (Ligands)
RN - 0 (Mannose-Binding Lectins)
RN - 0 (Oligosaccharides)
RN - 31103-86-3 (Mannose)
SB - IM