paratope

Thus these regions are the paratope, the binding site of antigen.

The part of an antibody that recognizes the epitope is called a 'paratope'.

By contrast, linear epitopes interact with the paratope based on their primary structure.

Likewise, it is only paratope of the antibody that comes in contact with the epitope.

A paratope, also called an antigen-binding site, is a part of an antibody which recognizes and binds to an antigen.

These epitopes interact with the paratope based on the 3-D surface features and shape or tertiary structure of the antigen.

He also defined the "paratope" to be that part of an antibody variable region that binds to an antigen.

That molecular region which binds to-or, in jargon, ligates-the epitope is the paratope.

A set of CDRs constitutes a paratope.

The paratope on the B cell receptor comes in contact only with those amino acids that lie on the "surface" of the protein.

The paratope is shaped at the amino terminal end of the antibody monomer by the variable domains from the heavy and light chains.

Each such mutation alters the epitope-binding ability of the paratope slightly, creating new clones of B cells in the process.

The best developed version of immune network theory is called the symmetrical network theory, in which the distinction between idiotype and paratope plays no role.

Such discontinuous amino acids that come together in three-dimensional conformation and interact with the receptor's paratope are called conformational epitopes.

The antigenic determinant or epitope is recognized by the paratope of antibody, situated at the variable region of the polypeptide chain.

The engraved inner portions of idiotype (encircled region no.5) is the paratope where the epitope of the antigen binds.

Each arm of the Y shape of an antibody monomer is tipped with a paratope, which is a set of complementarity determining regions.

If an antibody binds to an antigen's epitope, the paratope could become the epitope for another antibody that will then bind to it.

The variable domain contains the paratope (the antigen-binding site), comprising a set of complementarity determining regions, at the amino terminal end of the monomer.

The epitopes of protein antigens are divided into two categories, conformational epitopes and linear epitopes, based on their structure and interaction with the paratope.

As an example, affinity is the binding strength between the complex structures of the epitope of antigenic determinant and paratope of antigen-binding site of an antibody.

Each of the two tips of Fab region is the paratope, which binds a matching molecular sequence and its 3D shape (conformation), altogether called epitope, within the target antigen.

When the paratope of Ig class gamma (IgG) binds its matching epitope, IgG's Fc region conformationally shifts and can host a complement protein, initiating the complement cascade that terminates by punching a hole in a cell membrane.