Immunoglobulin kappa variable 5-2

Definition:

V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.

References:

[1]. Grace Teng, et al. Immunoglobulin somatic hypermutation. Annu Rev Genet. 2007;41:107-20. [Content Brief]

[2]. Michael McHeyzer-Williams, et al. Molecular programming of B cell memory. Nat Rev Immunol. 2011 Dec 9;12(1):24-34. [Content Brief]

[3]. Harry W Schroeder Jr, et al. Structure and function of immunoglobulins. J Allergy Clin Immunol. 2010 Feb;125(2 Suppl 2):S41-52. [Content Brief]

[4]. Marie-Paule Lefranc, et al. Immunoglobulin and T Cell Receptor Genes: IMGT(®) and the Birth and Rise of Immunoinformatics. Front Immunol. 2014 Feb 5;5:22. [Content Brief]

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