Immunoglobulin heavy constant gamma 2 (Ig gamma-2 chain C region) (Ig gamma-2 chain C region DOT) (Ig gamma-2 chain C region TIL) (Ig gamma-2 chain C region ZIE)
1_ASTKG 6_ PSVFP 11_ LAPCS 16_ RSTSE 21_ STAAL 26_ GCLVK 31_ DYFPE 36_ PVTVS 41_ WNSGA 46_ LTSGV 51_ HTFPA 56_ VLQSS 61_ GLYSL 66_ SSVVT 71_ VPSSN 76_ FGTQT 81_ YTCNV 86_ DHKPS 91_ NTKVD 96_ KTVER 101_ KCCVE 106_ CPPCP 111_ APPVA 116_ GPSVF 121_ LFPPK 126_ PKDTL 131_ MISRT 136_ PEVTC 141_ VVVDV 146_ SHEDP 151_ EVQFN 156_ WYVDG 161_ VEVHN 166_ AKTKP 171_ REEQF 176_ NSTFR 181_ VVSVL 186_ TVVHQ 191_ DWLNG 196_ KEYKC 201_ KVSNK 206_ GLPAP 211_ IEKTI 216_ SKTKG 221_ QPREP 226_ QVYTL 231_ PPSRE 236_ EMTKN 241_ QVSLT 246_ CLVKG 251_ FYPSD 256_ ISVEW 261_ ESNGQ 266_ PENNY 271_ KTTPP 276_ MLDSD 281_ GSFFL 286_ YSKLT 291_ VDKSR 296_ WQQGN 301_ VFSCS 306_ VMHEA 311_ LHNHY 316_ TQKSL 321_SLSPG
1: Constant region of immunoglobulin heavy chains. 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)