cd07699: IgC_L (this model, PSSM-Id:143323 is obsolete and has been replaced by 409496)
Immunoglobulin Constant domain
IgC_L: Immunoglobulin (Ig) light chain constant (C) domain. The basic structure of Ig molecules is a tetramer of two light chains and two heavy chains linked by disulfide bonds. In Ig, each chain is composed of one variable domain (IgV) and one or more constant domains (IgC); these names reflect the fact that the variability in sequences is higher in the variable domain than in the constant domain. There are five types of heavy chains (alpha, gamma, delta, epsilon, and mu), which determine the type of immunoglobulin: IgA, IgG, IgD, IgE, and IgM, respectively. In higher vertebrates, there are two types of light chain, designated kappa and lambda, which seem to be functionally identical, and can associate with any of the heavy chains.
Structure:1RHH_A; human light chain IgC domain forms a heterodimer with the CH1 domain of the heavy chain, defined using 4.0 A contacts. - View structure with Cn3D
Jiyao W et al.(2023). "The conserved domain database in 2023.",