Epitopes: Difference between revisions
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Antibody epitopes can occur on the surfaces of natively folded proteins, or equally well on denatured conformations of proteins. Peptides, sometimes too short to have a well-defined fold, can bind to antibodies. T cell epitopes are always peptide fragments, and hence, represent a denatured (unfolded) form of the native protein. | Antibody epitopes can occur on the surfaces of natively folded proteins, or equally well on denatured conformations of proteins. Peptides, sometimes too short to have a well-defined fold, can bind to antibodies. T cell epitopes are always peptide fragments, and hence, represent a denatured (unfolded) form of the native protein. | ||
==Epitope Prediction Servers== | |||
A common way to identify the epitope recognized by a particular antibody is to display random peptides (for example, using phage display libraries), and then to identify the sequences of the peptides with the highest affinity for the antibody. These sequences can then be used to predict where the epitope lies on the native protein, taking into account that the epitope on the native protein may be discontinuous. In this strategy, the 3D structure of the protein antigen must be known. | |||
===[http://curie.utmb.edu/episearch.html EpiSearch]] requires as input the sequences of peptides that bind to the antibody in question, and the 3D structure ([[PDB code]] of the protein antigen. | |||
==References and Notes== | ==References and Notes== | ||
<references /> | <references /> | ||
