An epitope is a component of an antigen that is recognized by antibody or host system and often called “antigen determinantâ€Â. Epitopes are non-self proteins and consist of large amino acid sequences, these sequences either are continuous or discontinuous chains which will offer the binding sites to antibodies. These molecules show high degree specificity in reactions and well-known example for cross-reactivity. Immunome Research Journal offers new trends in Immunology. The journal aims to integrate both conventional immunological aspects and modern computational and It provides new insights in structure predictions of immune systems such as immune Epitopes and receptor molecules.
The epitopes of protein antigens are divided into two categories, conformational epitopes and linear epitopes, based on their structure and interaction with the paratope.Conformational and linear epitopes interact with the paratope based on the 3-D conformation adopted by the epitope, which is determined by the surface features of the involved epitope residues and the shape or tertiary structure of other segments of the antigen. A conformational epitope is formed by the 3-D conformation adopted by the interaction of discontiguous amino acid residues. In contrast, a linear epitope is formed by the 3-D conformation adopted by the interaction of contiguous amino acid residues. A linear epitope is not determined solely by the primary structure of the involved amino acids. Residues that flank such amino acid residues, as well as more distant amino acid residues of the antigen affect the ability of the primary structure residues to adopt the epitope's 3-D conformation.The proportion of epitopes that are conformational is unknown