Introduction -- FASTA -- BLAST -- Modular Domain -- Multiple Sequence Alignment -- PDB -- Summary

Summary

The insulin receptor is a fascinating player in the family of kinase receptors, and performs a pinnacle role not only in the homeostasis of glucose levels but also offers another alternative in which to activate the enzyme phosphatidylinositol 3'-kinase, resulting in amplified rates of cell proliferation. It has been observed that the insulin receptor exists in 2 main isoforms, denoted isoform A (IR-A) and B (IR-B), each with potentially differing insulin affinities. The insulin receptor is also related very much so to another multidomain homologous protein (such as itself), t he insulin-like growth factor receptor (IGF-1R) . Analysis of the proteins complex structure reveals a series of domains that have been conserved, in addition to its phylogenetically ancient tyrosine kinase domain. These are demonstrated in the multiple sequence alignments. The tyrosine kinase domain alignment shows a strong preference for tyrosine substrates, as opposed to serine or Threonine residues. The insulin receptor provides a clear example of a transmembrane tetramer receptor molecule involved in the transduction and translocation of a large array of signals across differing cellular pathways.

Produced by

Kelly Thorneycroft, Omar Jamshad, Rich Wang and Duvaraka Kulaveerasingam