Modes of association of concanavalin A with alpha-D-glycosides.

Complexes of Con A with alpha-D-glycosides were studied using 1H-NMR, ESR and fluorescence methods. Correlation times, tau c, for the interaction of the aglycon protons with the manganese ion, present at the S1 site of the protein, were calculated from T1 measurements at two frequencies. The protons of aromatic aglycons have tau c values comparable to the rotational correlation time of the protein molecule, whereas those of non-aromatic aglycons have tau cs 10 to 100 times lower. The correlation times were combined with the experimentally acquired paramagnetic contributions to proton relaxation due to the presence of the manganese ion to yield manganese-proton distances. These distances show that aromatic aglycons have additional favorable contacts with the protein which stabilize the lectin-saccharide interaction. The results are compared to the crystal structure of the methyl alpha-D-glycopyranoside complex with Con A and to models earlier proposed for the binding of monosaccharides to Con A.