1Q8K

Solution structure of alpha subunit of human eIF2


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 51 
  • Conformers Submitted: 15 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Solution Structure of Human Initiation Factor eIF2alpha Reveals Homology to the Elongation Factor eEF1B.

Ito, T.Marintchev, A.Wagner, G.

(2004) Structure 12: 1693-1704

  • DOI: https://doi.org/10.1016/j.str.2004.07.010
  • Primary Citation of Related Structures:  
    1Q8K

  • PubMed Abstract: 

    The GTP-bound form of the trimeric eukaryotic translation initiation factor 2 (eIF2) transfers aminoacylated initiator methionyl tRNA onto the 40S ribosome. We have solved with solution NMR the structure of the alpha subunit of human eIF2 (heIF2alpha). The protein consists of two domains that are mobile relative to each other. The N-terminal domain has an S1-type oligonucleotide/oligosaccharide binding-fold subdomain and an alpha-helical subdomain. The C-terminal domain adopts an alphabeta-fold very similar to the C-terminal domain of elongation factor (eEF) 1Balpha, the guanine-nucleotide exchange factor for eEF1A. The structural and functional similarities found between eIF2alpha/eIF2gamma and eEF1Balpha/eEF1A suggest a model for the interaction of eIF2alpha with eIF2gamma, and eIF2 with Met-tRNAiMet. It further indicates a previously unrecognized evolutionary lineage of eIF2alpha/gamma from the functionally related elongation factor eEF1Balpha/eEF1A complex.


  • Organizational Affiliation

    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Eukaryotic translation initiation factor 2 subunit 1308Homo sapiensMutation(s): 3 
Gene Names: EIF2S1 OR EIF2A
UniProt & NIH Common Fund Data Resources
Find proteins for P05198 (Homo sapiens)
Explore P05198 
Go to UniProtKB:  P05198
PHAROS:  P05198
GTEx:  ENSG00000134001 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP05198
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 51 
  • Conformers Submitted: 15 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2004-09-07
    Type: Initial release
  • Version 1.1: 2008-04-29
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2021-10-27
    Changes: Database references, Derived calculations