InterPro domain: IPR043510

The basic leucine zipper and W2 domain-containing proteins 1 and 2 (BZW1 and BZW2), also known as eIF5-mimic proteins, are paralogous human proteins containing C-terminal HEAT domains that resemble the HEAT domain of eIF5 [ 1 ]. BZW1 plays an important role in the cell cycle and transcriptionally control the histone H4 gene during G1/S phase [ 2 ]. The Drosophila ortholog, kra (krasavietz) or exba (extra bases), may be involved in translational inhibition in neural development. The structure of this C-terminal W2 domain resembles that of a set of concatenated HEAT repeats [ 3 , 4 , 5 ].

The W2 domain has a globular fold and is exclusively composed out of alpha-helices [ 6 , 7 , 8 ]. 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.

1. Translational autoregulation of BZW1 and BZW2 expression by modulating the stringency of start codon selection. PLoS ONE 13, e0192648
2. Overexpression of BZW1 is an independent poor prognosis marker and its down-regulation suppresses lung adenocarcinoma metastasis. Sci Rep 9, 14624
3. Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system. Genome Res. 10, 1172-84
4. A eukaryotic initiation factor 5C is upregulated during metamorphosis in the cotton bollworm, Helicoverpa armigera. BMC Dev. Biol. 9, 19
5. The F-actin-microtubule crosslinker Shot is a platform for Krasavietz-mediated translational regulation of midline axon repulsion. Development 134, 1767-77
6. Structure of the catalytic fragment of translation initiation factor 2B and identification of a critically important catalytic residue. J. Biol. Chem. 279, 10584-92
7. Crystal structure of the C-terminal domain of S.cerevisiae eIF5. J. Mol. Biol. 359, 1-9
8. The crystal structure of the carboxy-terminal domain of human translation initiation factor eIF5. J. Mol. Biol. 360, 457-65