Ire1: Difference between revisions

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<StructureSection load='3lj0' size='400' side='right' caption='Structure of yeast Ire1 cytoplasmic domain dimer complex with quercetin, ADP (stick model), Ca+2 and Sr+2 ions (PDB entry [[3lj0]])' scene=''>
<StructureSection load='3lj0' size='400' side='right' caption='Structure of yeast Ire1 cytoplasmic domain dimer complex with quercetin, ADP, Ca+2 and Sr+2 ions (PDB entry [[3lj0]])' scene='51/516469/Cv/1'>
== Function ==   
== Function ==   
'''Ire1''' is a serine/threonine protein kinase/endoribonuclease.  It is important in altering gene expression as a response to endoplasmic reticulum-based stress signals<ref>PMID:11034898</ref>.  The endoribonuclase domain of Ire1 is a transcriptional activator which triggers growth arrest and apoptosis.  The kinase domain of Ire1 is required for activation of the endoribonuclase domain.  Ire1 senses unfolded proteins causing its auto-activation.  
'''Ire1''' is a serine/threonine protein kinase/endoribonuclease.  It is important in altering gene expression as a response to endoplasmic reticulum-based stress signals<ref>PMID:11034898</ref>.  The endoribonuclase domain of Ire1 is a transcriptional activator which triggers growth arrest and apoptosis.  The kinase domain of Ire1 is required for activation of the endoribonuclase domain.  Ire1 senses unfolded proteins causing its auto-activation.  
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== Structural highlights ==
== Structural highlights ==


Yeast Ire1 structure contains 3 phosphorylated residues: 2 Ser and a Thr.  Iew1 shows a different binding site for ADP and for quercetin.  Quercetin is a powerful activator of Ire1.  Ire1 binds 2 molecules of quercetin at its dimer interface<ref>PMID:23880584</ref>.  
Yeast Ire1 structure contains 3 phosphorylated residues: 2 Ser and a Thr.  Ire1 shows a different binding site for ADP and for quercetin.  Quercetin is a powerful activator of Ire1.  Ire1 binds 2 molecules of quercetin at its dimer interface<ref>PMID:23880584</ref>.  


==3D structures of Ire1==
==3D structures of Ire1==