| First Author | Arai M | Year | 2010 |
| Journal | FEBS Lett | Volume | 584 |
| Issue | 22 | Pages | 4500-4 |
| PubMed ID | 20969867 | Mgi Jnum | J:167070 |
| Mgi Id | MGI:4867123 | Doi | 10.1016/j.febslet.2010.10.024 |
| Citation | Arai M, et al. (2010) Leu628 of the KIX domain of CBP is a key residue for the interaction with the MLL transactivation domain. FEBS Lett 584(22):4500-4 |
| abstractText | Physical interaction between the transactivation domain (TAD) of the mixed-lineage leukemia protein (MLL) and the KIX domain of the cyclic-AMP response element binding protein (CREB) binding protein (CBP) is necessary for MLL-mediated transcriptional activation. We show by alanine-scanning mutagenesis that hydrophobic surface residues of KIX, especially L628, are energetically important for binding the MLL TAD. NMR studies of the KIX-L628A mutant suggest that L628 plays a crucial role in conformational transitions at the MLL binding site, necessary for high affinity interactions with MLL. Unexpectedly, MLL also binds to the c-Myb/phosphorylated kinase-inducible domain of CREB (pKID) site of KIX, highlighting the complex nature of interactions involving intrinsically disordered transcriptional activators. |
