(Q27642510)

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The Crystal Structure of the N-terminal Region of the Alpha Subunit of Translation Initiation Factor 2 (eIF2α) from Saccharomyces cerevisiae Provides a View of the Loop Containing Serine 51, the Target of the eIF2α-specific Kinases

scientific article published on November 21, 2003

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The crystal structure of the N-terminal region of the alpha subunit of translation initiation factor 2 (eIF2alpha) from Saccharomyces cerevisiae provides a view of the loop containing serine 51, the target of the eIF2alpha-specific kinases (English)

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The Crystal Structure of the N-terminal Region of the Alpha Subunit of Translation Initiation Factor 2 (eIF2α) from Saccharomyces cerevisiae Provides a View of the Loop Containing Serine 51, the Target of the eIF2α-specific Kinases (English)

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10.1016/J.JMB.2003.09.045

https://api.crossref.org/works/10.1016/J.JMB.2003.09.045

30 March 2024

crystal structure

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Saccharomyces cerevisiae

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structural biology

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author name string

Simrit Dhaliwal

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David W. Hoffman

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A14607111

30 March 2024

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publication date

21 November 2003

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full work available at URL

https://api.elsevier.com/content/article/PII:S002228360301194X?httpAccept=text/xml

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10.1016/J.JMB.2003.09.045

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https://api.elsevier.com/content/article/PII:S002228360301194X?httpAccept=text/plain

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10.1016/J.JMB.2003.09.045

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Journal of Molecular Biology

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334

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2

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187-95

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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20 May 2022

https://opencitations.net/index/coci/api/v1/citations/10.1107/S0907444998003254

Molecular mechanisms of translation initiation in eukaryotes

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Eukaryotic translation initiation factors and regulators

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Amino acid sequence analysis of the beta- and gamma-subunits of eukaryotic initiation factor eIF-2. Identification of regions interacting with GTP

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eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange.

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Tight binding of the phosphorylated alpha subunit of initiation factor 2 (eIF2alpha) to the regulatory subunits of guanine nucleotide exchange factor eIF2B is required for inhibition of translation initiation

8

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Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

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Gcn4p, a master regulator of gene expression, is controlled at multiple levels by diverse signals of starvation and stress

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The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.

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Structure of the beta subunit of translation initiation factor 2 from the archaeon Methanococcus jannaschii: a representative of the eIF2beta/eIF5 family of proteins

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Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2alpha

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OB(oligonucleotide/oligosaccharide binding)-fold: common structural and functional solution for non-homologous sequences

17

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The eIF1A solution structure reveals a large RNA-binding surface important for scanning function

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The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif

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Themes in RNA-protein recognition.

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Ribosomal protein S17: Characterization of the three-dimensional structure by proton and nitrogen-15 NMR

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The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold

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Translational initiation factors IF-1 and eIF-2α share an RNA-binding motif with prokaryotic ribosomal protein S1 and polynucleotide phosphorylase

23

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Universally conserved translation initiation factors

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Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation

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Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alpha.

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Structural basis for control by phosphorylation

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Protein kinase phosphorylation site sequences and consensus specificity motifs: tabulations

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The alpha-helix dipole and the properties of proteins

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Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr

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Processing of X-ray diffraction data collected in oscillation mode

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