W2 domain
IPR003307
Definition
Translation initiation is a sophisticated, well regulated and highly coordinated cellular process in eukaryotes, in which at least 11 eukaryotic 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 [[cite:PMID:8520487], [cite:PMID:10958635], [cite:PMID:14681227], [cite:PMID:16616930], [cite:PMID:16781736]]: Eukaryotic translation initiation factor 2B epsilon (eIF-2B-epsilon). Eukaryotic translation initiation factor 4 gamma (eIF-4-gamma). 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 [[cite:PMID:14681227], [cite:PMID:16616930], [cite:PMID:16781736]]. 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.
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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