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Previous data from our group has shown that common HLA-DR molecules bind to multiple peptides encoded in the vaccine [32].
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The PDZ domains of syntenin bind to multiple peptide motifs with low-to-medium affinity [ 8, 9], are essential for assembly and organization of diverse cell-signaling processes occurring at the plasma membrane [ 6, 10].
In their role as housekeeping proteins and chaperones, hsp's can bind to multiple intracellular peptides including tumour peptides (Gething and Sambrook, 1992; Parsell and Lindquist, 1993).
Consider for example, the problem of predicting promiscuous MHC binding peptides [33], where each peptide can bind to multiple HLA molecules.
For example, peptide epitopes from pathogen antigens that bind to multiple MHC allotypes present in a population are needed for developing vaccines with broad protective immunity.
Some will respond to multiple peptides, others probably to fewer peptides.
Previous studies report heterogeneity of domains or proteins to bind multiple peptides (e. g., at least 13 different types of peptides have been reported to bind to SH3 domains [19]).
On the other hand, DII contains many cross-reactive epitopes eliciting neutralizing and non-neutralizing monoclonal antibodies that bind to fusion peptides, while DIII contains multiple type and subtype specific epitopes and several conformational virus-neutralizing epitopes [31], [32].
The aims here were to evaluate the LRRs ability to; homo-dimerize; bind larger proteins; and bind to small peptides.
These binding constants were within physiological ranges and suggest the LRR domain can bind multiple peptide ligands.
Consequently, all selected proteins bound to the VSL12 peptide but did not bind to other nonrelated peptides (Fig. 6).
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