The former forms a type 1 transmembrane receptor protein, and is typically located on the outer surface of these lymphocyte cells.
[1] Through biochemical signaling and by physically acquiring antigens from the immune synapses, the BCR controls the activation of the B cell.
[1] B cells' mechanical activity adheres to a pattern of negative and positive feedbacks that regulate the quantity of removed antigen by manipulating the dynamic of BCR–antigen bonds directly.
[1][3] The BCR can be found in a number of identical copies of membrane proteins that are exposed at the cell surface.
[1][7] Heterodimers may exist in the B cells as either an association or combination with another pre B cell-specific proteins or alone, thereby replacing the mIgM molecule.
There are a number of genes that encode each of these regions in the genome and can be joined in various ways to generate a wide range of receptor molecules.
The short JH (joining) and DH (diversity) regions are recombined first in early pro-B cells in a process that is dependent on the enzymes RAG2 and RAG1.
[1][5] However, there is a distinctive structural dissimilarity in the C-terminal area of the heavy chains, as it consists of a hydrophobic stretch that is short, which spreads across the lipid bilayer of the membrane.
[11] The binding event allows phosphorylation of immunoreceptor tyrosine-based activation motifs (ITAMs) in the associated Igα/Igβ heterodimer subunits by the tyrosine kinases of the Src family, including Blk, Lyn, and Fyn.