Immunoglobulin kappa variable 1-39 (Ig kappa chain V-I region DEE) (Ig kappa chain V-I region Hau) (Ig kappa chain V-I region Mev) (Ig kappa chain V-I region OU) (Ig kappa chain V-I region Walker)
1_MDMRV 6_ PAQLL 11_ GLLLL 16_ WLRGA 21_ RCDIQ 26_ MTQSP 31_ SSLSA 36_ SVGDR 41_ VTITC 46_ RASQS 51_ ISSYL 56_ NWYQQ 61_ KPGKA 66_ PKLLI 71_ YAASS 76_ LQSGV 81_ PSRFS 86_ GSGSG 91_ TDFTL 96_ TISSL 101_ QPEDF 106_ ATYYC 111_QQSYS
1: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). 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 (PubMed:20176268, PubMed:22158414). 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 (PubMed:17576170, PubMed:20176268)