ArticleProtein & cell2010
Crystal structure of the C-terminal domain of the ɛ subunit of human translation initiation factor eIF2B.
Article in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 19 citations in OpenAlex.
- Comparative Transcriptome Analysis on the Regulatory Mechanism of Thoracic Ganglia inLife (Basel, Switzerland) · 2022Article
- The metaphorical swiss army knife: The multitude and diverse roles of HEAT domains in eukaryotic translation initiation.Nucleic acids research · 2022Review
- The PCI domains are "winged" HEAT domains.PloS one · 2022Article
- Article
- Vanishing white matter: Eukaryotic initiation factor 2B model and the impact of missense mutations.Molecular genetics & genomic medicine · 2021Article
- eIF2B and the Integrated Stress Response: A Structural and Mechanistic View.Biochemistry · 2020Article
- eIF2B-catalyzed nucleotide exchange and phosphoregulation by the integrated stress response.Science (New York, N.Y.) · 2019Article
- Novel mechanisms of eIF2B action and regulation by eIF2α phosphorylation.Nucleic acids research · 2017Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
Eukaryotic translation initiation factor eIF2B, the guanine nucleotide exchange factor (GEF) for eIF2, catalyzes conversion of eIF2·GDP to eIF2·GTP. The eIF2B is composed of five subunits, α, β, γ, δ and ɛ, within which the ɛ subunit is responsible for catalyzing the guanine exchange reaction. Here we present the crystal structure of the C-terminal domain of human eIF2Bɛ (eIF2Bɛ-CTD) at 2.0-Å resolution. The structure resembles a HEAT motif and three charge-rich areas on its surface can be identified. When compared to yeast eIF2Bɛ-CTD, one area involves highly conserved AA boxes while the other two are only partially conserved. In addition, the previously reported mutations in human eIF2Bɛ-CTD, which are related to the loss of the GEF activity and human VWM disease, have been discussed. Based on the structure, most of such mutations tend to destabilize the HEAT motif.
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