| Tdark | Immunoglobulin heavy variable 3-48 |
V region of the variable domain of immunoglobulin heavy 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 (PubMed:22158414, PubMed:20176268). 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:20176268, PubMed:17576170).
Comments
| PMID | Year | Title |
|---|---|---|
| 22158414 | 2011 | Molecular programming of B cell memory. |
| 20176268 | 2010 | Structure and function of immunoglobulins. |
| 17576170 | 2007 | Immunoglobulin somatic hypermutation. |
| 12508121 | 2003 | The DNA sequence and analysis of human chromosome 14. |
| 11340299 | 2001 | Nomenclature of the human immunoglobulin heavy (IGH) genes. |
| 9841928 | 1998 | The complete nucleotide sequence of the human immunoglobulin heavy chain variable region locus. |
| 9614934 | 1998 | Myosin-reactive autoantibodies in rheumatic carditis and normal fetus. |
| 8490662 | 1993 | Structure and physical map of 64 variable segments in the 3'0.8-megabase region of the human immunoglobulin heavy-chain locus. |
| 6410398 | 1983 | Amino acid sequence of the Fv region of a human monoclonal IgM (protein WEA) with antibody activity against 3,4-pyruvylated galactose in Klebsiella polysaccharides K30 and K33. |
