Insulin receptor
From Proteopedia
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| - | <StructureSection load='3bu5' size='400' side='right' caption='Structure of human insulin receptor tyrosine kinase catalytic domain complex with peptide (green) and ATP (PDB entry [[3bu5]])' scene=''> | + | <StructureSection load='3bu5' size='400' side='right' caption='Structure of human insulin receptor tyrosine kinase catalytic domain complex with insulin receptor substrate 2 peptide (green), Mg+2 ion (green) and ATP (stick model) (PDB entry [[3bu5]])' scene=''> |
'''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, IGF-I and IGF-II. IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetics and cancer. The IR is a dimer where each monomer contains 8 distinct domains. The beta-chain contains a tyrosine kinase catalytic domain (TK). | '''Insulin receptor''' (IR) is a transmembrane receptor activated by insulin, IGF-I and IGF-II. IR is important for the regulation of glucose homeostasis and its malfunction can cause diabetics and cancer. The IR is a dimer where each monomer contains 8 distinct domains. The beta-chain contains a tyrosine kinase catalytic domain (TK). | ||
Revision as of 09:34, 18 December 2013
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Michal Harel, Alexander Berchansky, Angel Herraez, R. Jeremy Johnson, Karsten Theis, Jaime Prilusky
