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PROSITE documentation PDOC51363 [for PROSITE entry PS51363]

W2 domain profile





Description

Translation initiation is a sophisticated, well regulated and highly coordinated cellular process in eukaryotes, in which at least 11 eukayrotic initiation factors (eIFs) are included. The W2 domain (two invariant tryptophans) is a region of ~165 amino acids which is found in the C-terminus of the following eIFs [1,2,3,4,5]:

  • Eukaryotic translation initiation factor 2B epsilon (eIF-2B-epsilon).
  • Eukaryotic translation initiation factor 4 γ (eIF-4-γ).
  • Eukaryotic translation initiation factor 5 (eIF-5), a GTPase-activating protein (GAP) specific for eIF2.

The W2 domain has a globular fold and is exclusively composed out of α-helices (see <PDB:2FUL>) [3,4,5]. The structure can be divided into a structural C-terminal core onto which the two N-terminal helices are attached. The core contains two aromatic/acidic residue-rich regions (AA boxes), which are important for mediating protein-protein interactions.

The profile we developed covers the entire W2 domain.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Last update:

March 2008 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

W2, PS51363; W2 domain profile  (MATRIX)


References

1AuthorsKoonin E.V.
TitleMultidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs.
SourceProtein Sci. 4:1608-1617(1995).
PubMed ID8520487

2AuthorsAravind L. Koonin E.V.
TitleEukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.
SourceGenome Res. 10:1172-1184(2000).
PubMed ID10958635

3AuthorsBoesen T. Mohammad S.S. Pavitt G.D. Andersen G.R.
TitleStructure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue.
SourceJ. Biol. Chem. 279:10584-10592(2004).
PubMed ID14681227
DOI10.1074/jbc.M311055200

4AuthorsWei Z. Xue Y. Xu H. Gong W.
TitleCrystal structure of the C-terminal domain of S.cerevisiae eIF5.
SourceJ. Mol. Biol. 359:1-9(2006).
PubMed ID16616930
DOI10.1016/j.jmb.2006.03.037

5AuthorsBieniossek C. Schuetz P. Bumann M. Limacher A. Uson I. Baumann U.
TitleThe crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5.
SourceJ. Mol. Biol. 360:457-465(2006).
PubMed ID16781736
DOI10.1016/j.jmb.2006.05.021



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

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