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Ire1
From Proteopedia
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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 (stick model), Ca+2 and Sr+2 ions (PDB entry [[3lj0]])' scene=''> | ||
| - | + | == 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: | + | '''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:23880584</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 == | ||
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| + | Yeast Ire1 structure 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== | ||
Revision as of 06:43, 3 April 2016
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