Insulin receptor

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<StructureSection load='3bu5' size='400' side='right' caption='Structure of human insulin receptor tyrosine kinase catalytic domain complex with insulin receptor substrate 2 peptide (cyan), Mg+2 ion (green) and ATP (PDB entry [[3bu5]])' scene='51/516456/Cv/1'>
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<StructureSection load='3bu5' size='450' side='right' caption='Structure of human insulin receptor tyrosine kinase catalytic domain complex with insulin receptor substrate 2 peptide (cyan), Mg+2 ion (green) and ATP (PDB entry [[3bu5]])' scene='51/516456/Cv/1'>
== Function ==
== Function ==
'''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, insulin-like growth factor I and II<ref>PMID:8141246</ref>. The IR is a dimer where each monomer contains 8 distinct domains. The β-chain contains a tyrosine kinase catalytic domain (TK). For more details see [[Student Projects for UMass Chemistry 423 Spring 2012-1]].<br />
'''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, insulin-like growth factor I and II<ref>PMID:8141246</ref>. The IR is a dimer where each monomer contains 8 distinct domains. The β-chain contains a tyrosine kinase catalytic domain (TK). For more details see [[Student Projects for UMass Chemistry 423 Spring 2012-1]].<br />
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TK domain of IR contains an activation loop and a catalytic loop and 3 phosphorylated tyrosine residues. The bound IR substrate 2 peptide tyrosine is the phosphorylated residue<ref>PMID:18278056</ref>.
TK domain of IR contains an activation loop and a catalytic loop and 3 phosphorylated tyrosine residues. The bound IR substrate 2 peptide tyrosine is the phosphorylated residue<ref>PMID:18278056</ref>.
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<scene name='51/516456/Cv/6'>ATP/Mg binding site</scene>.
See also [[Insulin Receptor - kinase domain (hebrew)]] and [[Insulin receptor (Hebrew)]].
See also [[Insulin Receptor - kinase domain (hebrew)]] and [[Insulin receptor (Hebrew)]].

Revision as of 11:13, 5 April 2016

Structure of human insulin receptor tyrosine kinase catalytic domain complex with insulin receptor substrate 2 peptide (cyan), Mg+2 ion (green) and ATP (PDB entry 3bu5)

Drag the structure with the mouse to rotate

3D structures of insulin receptor

1irk – hIR TK domain – human
1i44, 1p14 – hIR TK domain (mutant)
2hr7 – hIR domains 1-3
2mfr – hIR transmembrane domain - NMR
4xlv - hIR TK domain (mutant) + ATP derivative
1ir3 - hIR TK domain (mutant) + ATP analog + peptide
3bu5, 3bu6 - hIR TK domain + ATP + peptide
3bu3 - hIR TK domain + peptide
1gag, 2z8c - hIR TK domain (mutant) + peptide
3ekk, 3ekn, 4ibm - hIR TK domain (mutant) + inhibitor
3eta - hIR TK domain + inhibitor
2dtg, 3loh - hIR ectodomain (mutant) + antibody
2auh – hIR TK domain + growth factor receptor-bound protein 14
2b4s - hIR TK domain + tyrosine-protein phosphatase
1rqq – hIR TK domain (mutant) + adaptor protein PS

References

  1. ↑ Lee J, Pilch PF. The insulin receptor: structure, function, and signaling. Am J Physiol. 1994 Feb;266(2 Pt 1):C319-34. PMID:8141246
  2. ↑ Frasca F, Pandini G, Sciacca L, Pezzino V, Squatrito S, Belfiore A, Vigneri R. The role of insulin receptors and IGF-I receptors in cancer and other diseases. Arch Physiol Biochem. 2008 Feb;114(1):23-37. doi: 10.1080/13813450801969715 . PMID:18465356 doi:http://dx.doi.org/10.1080/13813450801969715
  3. ↑ Wu J, Tseng YD, Xu CF, Neubert TA, White MF, Hubbard SR. Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2. Nat Struct Mol Biol. 2008 Mar;15(3):251-8. Epub 2008 Feb 17. PMID:18278056 doi:10.1038/nsmb.1388
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