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Griffin:Antibody Basics: Difference between revisions
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The general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures to exist. This region is known as the hypervariable region (Fab). Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction. | The general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures to exist. This region is known as the hypervariable region (Fab). Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction. | ||
===V(D)J recombination=== | |||
*[https://pubmed.ncbi.nlm.nih.gov/27729912/ Antigen-binding site variability] is achieved by [https://en.wikipedia.org/wiki/V(D)J_recombination V(D)J recombination]; heavy/light chain pair combinatorial diversity, post-activation [https://en.wikipedia.org/wiki/Somatic_hypermutation somatic hypermutation], and class switching ([https://en.wikipedia.org/wiki/Immunoglobulin_class_switching isotypic commutation]). | |||
===Fc fragment=== | ===Fc fragment=== | ||
