The binding of an antigen to the human B Cell receptor is identical to other common soluble antibodies (such as [https://en.wikipedia.org/wiki/Immunoglobulin_G IgG], [https://en.wikipedia.org/wiki/Immunoglobulin_A IgA], [https://en.wikipedia.org/wiki/Immunoglobulin_M IgM], [https://en.wikipedia.org/wiki/Immunoglobulin_E IgE], or [https://en.wikipedia.org/wiki/Immunoglobulin_D IgD]). The antibody portion of the B Cell Receptor is roughly "Y" shaped that consists of two identical heavy and two identical light chains creating two similar epitope or binding regions. Thus, two antigen molecules can bind independent of one another to produce the same response. Within this structure, there are both constant and variable regions. The stem of the "Y" is a constant region composed of only heavy chain interactions. ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fc]). The two heavy chains then branch at a flexible hinge region. These interact individually with one light chain creating the two fab fragments or branches of the "Y". Each Fab fragment contains a variable region ([https://en.wikipedia.org/wiki/Antibody#CDRs,_Fv,_Fab_and_Fc_Regions Fv]) and a constant region. The variable region that sits on top of the constant region in this fragment consists of hyper-variable loops which are random coils of amino acids that are unique to an antibody and allows specific recognition of an antigen. Furthermore, the light chains interact with the heavy chains via weak intermolecular forces and disulfide bridges.