paratope

(redirected from antigen-binding site)
Also found in: Dictionary, Thesaurus, Legal, Financial, Encyclopedia.
Related to antigen-binding site: variable region, Surface immunoglobulin

determinant

 [de-ter´mĭ-nant]
a factor that establishes the nature of an entity or event.
antigenic determinant a site on the surface of an antigen molecule to which a single antibody molecule binds; generally an antigen has several or many different antigenic determinants and reacts with many different antibodies. Called also epitope.
 Antigens contain antigenic determinants (epitopes) and antibodies contain antibody combining sites (paratopes). From Copstead and Banasik, 2000.
hidden determinant an antigenic determinant located in an unexposed region of a molecule so that it is prevented from interacting with receptors on lymphocytes, or with antibody molecules, and is unable to induce an immune response; it may appear following stereochemical alterations of molecular structure.
immunogenic determinant the part of an immunogenic molecule that interacts with a helper T cell in triggering antibody production as opposed to the antigenic determinant or hapten, which interacts with B cells.

par·a·tope

(par'ă-tōp),
That part of an antibody molecule composed of the variable regions of both the light and heavy chains that combine with the antigen.
[para- + -tope]

paratope

/para·tope/ (par´ah-tōp) the site on the antibody molecule that attaches to an antigen.

par·a·tope

(par'ă-tōp)
That part of an antibody molecule composed of the variable regions of both the light and heavy chains that combine with the antigen.
Synonym(s): antibody-combining site.

paratope

the site in the variable region of an antibody or T cell receptor that binds to an epitope of an antigen.
References in periodicals archive ?
This immune system shuffling is needed because the genes encoding antigen-binding sites come in pieces, which are known as V (for variable), D (for diversity), and J (for joining).
Antibody fragments are receiving increased attention as potential future biopharmaceuticals because, compared with monoclonal antibodies, they have a number of advantages such as improved tissue penetration and the ability to bind to targets inaccessible to conventional antigen-binding sites.

Full browser ?