Immunoglobulin domain

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Lua error in Module:Infobox at line 235: malformed pattern (missing ']'). 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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