Immunoglobulin domain

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Immunoglobulin domain
PDB 8fab EBI.jpg
Structure of an antigen binding fragment of an antibody.
Identifiers
Symbol ig
Pfam PF00047
Pfam clan CL0011
InterPro IPR013151
PROSITE PDOC00262
SCOP 8fab
SUPERFAMILY 8fab
CDD cd00096

The immunoglobulin domain is a type of protein domain that consists of a 2-layer sandwich of 7-9 antiparallel β-strands arranged in two β-sheets with a Greek key topology,[1][2] consisting of about 80 amino acids.

The backbone switches repeatedly between the two β-sheets. Typically, the pattern is (N-terminal β-hairpin in sheet 1)-(β-hairpin in sheet 2)-(β-strand in sheet 1)-(C-terminal β-hairpin in sheet 2). The cross-overs between sheets form an "X", so that the N- and C-terminal hairpins are facing each other.

Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin, and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein–protein and protein–ligand interactions.[3]

Examples

Human genes encoding proteins containing the immunoglobulin domain include:

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See also

References

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External links

This article incorporates text from the public domain Pfam and InterPro IPR013151

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