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3.1), and thus the ability to bind simultaneously to two identical structures.

However, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. Each of the branching chains comprising the y of an antibody contains a paratope that specifically binds to one particular epitope on an antigen, allowing the two molecules to bind together with precision. Each antibody contains two light chains that are always identical Other types of light chains, such as the iota (ι) chain, are found in lower vertebrates like chondrichthyes and teleostei. Each antibody class therefore has a valency, or number of binding sites available per antibody unit, which is typically the number of antibodies multiplied by two, as each antibody has two binding sites. Why do antibodies have 2 binding sites

Which two ig domains form the antigen binding site when joined together Which two ig domains extend the arms of the antibody away from the hinge region Which two ig domains attach to fc receptors on phagocytic cells and complement (initiates phagocytosis when ag is bound)

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