Immunoglobulin D (IgD)- Structure and Functions

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IgD is one of the five classes of immunoglobulins, which are proteins that function as antibodies in the immune system. Immunoglobulins are produced by B cells, a type of white blood cell, and can bind to specific antigens, such as bacteria, viruses, or toxins. By binding to antigens, immunoglobulins can mark them for destruction by other immune cells or neutralize their harmful effects.

IgD is a monomeric immunoglobulin, meaning that it consists of a single unit of four polypeptide chains: two identical heavy chains and two identical light chains. The heavy chains are of the delta (δ) class, which distinguishes IgD from other immunoglobulin classes. The light chains can be either kappa (κ) or lambda (λ) type, depending on the genetic rearrangement that occurs during B cell development.

The four chains are held together by disulfide bonds, which are covalent bonds between sulfur atoms. The disulfide bonds form between the heavy and light chains, as well as within each chain. The intrachain disulfide bonds divide each chain into domains, which are regions with a similar structure and function. The light chains have two domains: one variable (VL) and one constant (CL). The heavy chains have four domains: one variable (VH) and three constant (CH1, CH2, and CH3).

The variable domains of the heavy and light chains form the antigen binding site of IgD. Each IgD molecule has two antigen binding sites that can recognize the same antigen. The antigen binding site is also called the Fab (fragment antigen binding) region of IgD. The constant domains of the heavy chains form the Fc (fragment crystallizable) region of IgD, which can interact with other immune cells or molecules.

IgD can exist in two forms: membrane-bound or secreted. Membrane-bound IgD is expressed on the surface of mature B cells, along with IgM, another class of immunoglobulin. Membrane-bound IgD has an extra amino acid sequence at the C-terminal end of the CH3 domain that anchors it to the plasma membrane. It also associates with two accessory proteins called Ig-alpha and Ig-beta, which help transmit signals from IgD to the B cell.

Secreted IgD is released into the blood and mucosal secretions by a subset of B cells called IgD-secreting plasma cells. Secreted IgD does not have the extra amino acid sequence or the accessory proteins. It is a glycoprotein, meaning that it has sugar molecules attached to some of its amino acids. The sugar molecules may affect the stability and solubility of IgD.

The structure of IgD has some unique features that may influence its function. One of them is the long hinge region between the Fab and Fc regions. The hinge region is a flexible segment that allows IgD to bend and twist when binding to antigens. The hinge region also makes IgD more susceptible to proteolytic degradation by enzymes that can break down proteins.

The structure of IgD is summarized in the following diagram:

|------------------|------------------|
| | |
| | |
| | |
| VL VH | VL VH |
| | |
| | |
| | |
|------------------|------------------|
| CL | CL |
|------------------|------------------|
| CH1 | CH1 |
|------------------|------------------|
| CH2 | CH2 |
|------------------|------------------|
| CH3 | CH3 |
|------------------|------------------|
| C-terminal | C-terminal |
| sequence | sequence |
| (membrane- | (membrane- |
| bound only) | bound only) |
|------------------|------------------|