Inimmunology, aparatope, also known as anantigen-binding site, is the part of anantibody which recognizes and binds to anantigen.[1][2] It is a small region at the tip of the antibody'santigen-binding fragment and contains parts of the antibody'sheavy andlight chains.[1][2] Each paratope is made up of sixcomplementarity-determining regions - three from each of the light and heavy chains - that extend from a fold of anti-parallelbeta sheets.[2] Each arm of the Y-shaped antibody has an identical paratope at the end.[2]
Paratopes make up the parts of theB-cell receptor that bind to and make contact with theepitope of an antigen.[2] All the B-cell receptors on any one individualB cell have identical paratopes.[2] The uniqueness of a paratope allows it to bind to only one epitope with high affinity and as a result, each B cell can only respond to one epitope. The paratopes on B-cell receptors binding to their specific epitope is a critical step in theadaptive immune response.
The design and structure of paratopes can differ greatly between different species. In jawed-vertebrates,V(D)J recombination can result in billions of different paratopes.[3][4] The number of paratopes, however, is limited by the composition of the V, D, and J genes and the structure of the antibody.[3] Thus, many different species have developed ways to bypass this restriction and increase the diversity of possible paratopes.
In cows, an extra-long complementarity-determining region is considered to have an essential role in diversifying paratopes.[3][5] Additionally, both chickens and rabbits use gene conversion to increase the number of paratopes that are possible.[3]
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