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Signaling and Internalisation Function of the B Cell Antigen Receptor Complex

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Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 365))

Abstract

The mouse B-cell antigen receptor (BCR) is a multi-component transmembrane protein complex. This complex is comprised of the membrane-bound immunoglobulin (mIg) and the disulfide-linked Ig-α and Ig-β heterodimer which is non-covalently associated with all classes of mIg molecules,1 (for review see references 2–4). Ig-α and Ig-β are glycoproteins of Mr 34000 and Mr 39000,5,6,1 which are encoded by the B-cell specific genes mb-17 and B29,8 respectively. Both proteins carry extracellularly a glycosylated Ig-like domain, a single transmembrane region of 22 amino acids, and a cytoplasmic portion of either 61 or 48 amino acids. The transmembrane and the cytoplasmic part of Ig-α and Ig-β is strongly conserved between the mouse and the human proteins.9–13

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© 1994 Springer Science+Business Media New York

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Flaswinkel, H., Weiser, P., Kim, KM., Reth, M. (1994). Signaling and Internalisation Function of the B Cell Antigen Receptor Complex. In: Gupta, S., Paul, W.E., DeFranco, A., Perlmutter, R.M. (eds) Mechanisms of Lymphocyte Activation and Immune Regulation V. Advances in Experimental Medicine and Biology, vol 365. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0987-9_1

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  • DOI: https://doi.org/10.1007/978-1-4899-0987-9_1

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-0989-3

  • Online ISBN: 978-1-4899-0987-9

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