CD179a has an Ig V domain-like structure, but lacks the last beta-strand (beta7) of a typical V domain.

Instead, it has a carboxyl terminal end that shows no sequence homologies to any other proteins.

Though no CD179a-related human disease or pathology has been reported yet, the deficiency of other components of preB cell receptor such as CD179b, Ig mu heavy chain and CD79a has been shown to result in severe impairment of B cell development and agammaglobulinemia in human.

PreBCR transduces signals for: 1) cellular proliferation, differentiation from the proB cell to preB cell stage, 2) allelic exclusion at the Ig heavy chain gene locus, and 3) promotion of Ig light chain gene rearrangements.

[6] This article incorporates text from the United States National Library of Medicine, which is in the public domain.