Ferriheme dissociates from p-T-EIF2AK1:2xferriheme dimer

Stable Identifier
R-HSA-9648880
Type
Reaction [dissociation]
Species
Homo sapiens
Compartment
cytosol
ReviewStatus
5/5
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Ferriheme dissociates from p-T-EIF2AK1:2xferriheme dimer
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One molecule of hemin (ferriheme b chloride) tightly binds the N-terminal domain of EIF2AK1 (HRI) and one molecule of hemin loosely binds the kinase insert (KI) domain of EIF2AK1 (Bhavnani et al. 2018, and inferred from rabbit and mouse homologs). When cytosolic heme concentrations are low, heme dissociates from the KI domain, resulting in activation of the kinase activity of EIF2AK1 (inferred from rabbit and mouse homologs).
Literature References
PubMed ID Title Journal Year
28814160 Elucidation of molecular mechanism of stability of the heme-regulated eIF2α kinase upon binding of its ligand, hemin in its catalytic kinase domain

Pal, J, Bhavnani, V, Panigrahi, P, Kaviraj, S, Yapara, S, Suresh, CG

J. Biomol. Struct. Dyn. 2018
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Inferred From
Ferriheme dissociates from p-T-Eif2ak1:2xferriheme dimer (Mus musculus)
Ferriheme dissociates from p-T-EIF2AK1:2xferriheme dimer (Oryctolagus cuniculus)
Authored
May, B  (2019-06-10)
Reviewed
Chen, JJ  (2019-10-22)
Created
May, B  (2019-06-10)
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