Sentence examples for binding of the ley from inspiring English sources

Taken together with the established rigid nature of the Ley carbohydrate [26], the available data strongly supports the binding of the Ley antigen by the hu3S193 antibody to resemble the fit of an unbendable key into a rigid lock.

The chimeric (mouse/human) monoclonal IgG1 antibody BR96 (Seattle Genetics Inc., Seattle, WA) binding to the Ley was employed.

One water molecule in the unliganded hu3S193 binding site occupied a location (near tyrosines 32H and 33H) where the N-acetyl group of the Ley tetrasaccharide binds and could have been displaced during complex formation (Fig. 2 A and B).

Since hu3S193 binding of Ley was almost identical to that of the BR96 antibody, we proposed that the antibody response to this tumor-associated antigen was structurally conserved.

Approval of the "Ley Habilitante", or Enabling Act, was widely expected after the first reading on 14 November.

Similarly, the bound conformations of Ley in 1S3K and Fab1 were essentially the same (Table 2), which further supports the idea of the rigid character of the Ley carbohydrate determinant.

Apart from the subtle differences in solvent structure and minor adjustments of the Ley-specific Fuc residue, the binding sites for the three hu3S193 structures were identical (see Fig. 2 D).

Overlays of the hu3S193 Fab structures (two in complex with Ley and one unliganded Fab) demonstrate almost identical positions for all binding site residues in contact with the Ley tetrasaccharide (Fig. 2 D).

We have shown that the binding specificity for Ley by hu3S193 does not involve conformational changes and the interaction mimics the hydration patterns of free Ley antigens.

Binding changes of the individual mutants were determined using three saliva samples that are Lea (Nonsec/Lea), Ley (Sec/Ley) and Leb (Sec/Leb) positive, respectively (Fig. 8B).

There is no evidence of significant conformational changes occurring in either the Ley carbohydrate antigen or the hu3S193 binding site, which suggests a rigid fit binding mechanism.