Immunoglobulin superfamily
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Through Protein, Cell (biology) and Antibody
Immunoglobulin domains
Proteins of the IgSF possess a structural domain known as an immunoglobulin (Ig) domain. Ig domains are named after the immunoglobulin molecules. They contain about 70-110 amino acids and are categorized according to their size and function. Ig-domains possess a characteristic Ig-fold, which has a sandwich-like structure formed by two sheets of antiparallel beta strands. Interactions between hydrophobic amino acids on the inner side of the sandwich and highly conserved disulfide bonds formed between cysteine residues in the B and F strands, stabilize the Ig-fold.
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Classification
The Ig like domains can be classified as IgV, IgC1, IgC2, or IgI.
Most Ig domains are either variable (IgV) or constant (IgC).
- IgV: IgV domains with 9 beta strands are generally longer than IgC domains with 7 beta strands.
- IgC1 and IgC2: Ig domains of some members of the IgSF resemble IgV domains in the amino acid sequence, yet are similar in size to IgC domains. These are called IgC2 domains, while standard IgC domains are called IgC1 domains.
- IgI: Other Ig domains exist that are called intermediate (I) domains.
Members
The Ig domain was reported to be the most populous family of proteins in the human genome with 765 members identified. Members of the family can be found even in the bodies of animals with a simple physiological structure such as poriferan sponges. They have also been found in bacteria, where their presence is likely to be due to divergence from a shared ancestor of eukaryotic immunoglobulin superfamily domains.