| First Author | Park S | Year | 2013 |
| Journal | FEBS Lett | Volume | 587 |
| Issue | 16 | Pages | 2506-11 |
| PubMed ID | 23831576 | Mgi Jnum | J:199993 |
| Mgi Id | MGI:5506806 | Doi | 10.1016/j.febslet.2013.06.051 |
| Citation | Park S, et al. (2013) The CH2 domain of CBP/p300 is a novel zinc finger. FEBS Lett 587(16):2506-11 |
| abstractText | The transcriptional co-regulator CBP (CREB-binding protein) has a highly conserved cysteine/histidine-rich region (CH2) whose structure and function remain uncharacterized. Using nuclear magnetic resonance (NMR spectroscopy), sequence alignment, mass spectrometry, and mutagenesis, we show that the CH2 domain is not a canonical plant homeodomain (PHD) finger, as previously proposed, but binds an additional zinc atom through the region N-terminal to the putative PHD motif. The CH2 domain and the preceding bromodomain interact and mutually stabilize each other, implying a cooperative function. We tested the hypothesis that the bromodomain and the CH2 domain can interact with histones, but found that the CH2 does not participate in histone-recognition. |
