| First Author | Ito N | Year | 2009 |
| Journal | Genes Cells | Volume | 14 |
| Issue | 2 | Pages | 167-78 |
| PubMed ID | 19170764 | Mgi Jnum | J:146868 |
| Mgi Id | MGI:3838696 | Doi | 10.1111/j.1365-2443.2008.01259.x |
| Citation | Ito N, et al. (2009) Crystal structure of the Bach1 BTB domain and its regulation of homodimerization. Genes Cells 14(2):167-78 |
| abstractText | The BTB/POZ domain is known as a protein-protein interaction motif that mediates homodimer and higher order self-associations. Proteins containing the BTB domain exist throughout eukaryotes; however, there is little information about the mechanism that determines the oligomeric state of the BTB domain. To address this question, we have determined the X-ray structure of the mouse Bach1 BTB domain. The present structure is similar to the previously determined BTB domain folds, including the human Bach1 BTB domain; however, distinct structural features are present, such as a novel homodimer interaction surface. The homodimer formation was found to involve a novel hydrogen bond network and interactions between hydrophobic surfaces of the kinked N-terminus (N-hook) and the partner's C-terminal residues. The deletion of the N-hook resulted in the conversion of the homodimer into a monomer in solution, indicating that the N-hook promotes the homodimerization of the mBach1 BTB domain. We have also found that the BTB domain of Bach2, a protein highly related to Bach1, is present as a monomer due to a short peptide insertion at the N-hook. These results represent the first example of the key modulatory element of BTB domain homodimerization. |
