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 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.
Last update:
March 2008 / First entry.
Technical section
PROSITE method (with tools and information) covered by this documentation:
References
1
Authors
Koonin E.V.
Title
Multidomain organization of eukaryotic guanine nucleotide exchange translation initiation factor eIF-2B subunits revealed by analysis of conserved sequence motifs.
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