1MM3
Solution structure of the 2nd PHD domain from Mi2b with C-terminal loop replaced by corresponding loop from WSTF
Summary for 1MM3
| Entry DOI | 10.2210/pdb1mm3/pdb |
| Related | 1FP0 1MM2 1f62 |
| NMR Information | BMRB: 5556 |
| Descriptor | Mi2-beta(Chromodomain helicase-DNA-binding protein 4) and transcription factor WSTF, ZINC ION (2 entities in total) |
| Functional Keywords | phd, zinc finger, protein scaffold, dna binding protein-transcription complex, dna binding protein/transcription |
| Biological source | Homo sapiens (human) |
| Cellular location | Nucleus: Q14839 |
| Total number of polymer chains | 1 |
| Total formula weight | 6905.65 |
| Authors | Kwan, A.H.Y.,Gell, D.A.,Verger, A.,Crossley, M.,Matthews, J.M.,Mackay, J.P. (deposition date: 2002-09-02, release date: 2003-07-22, Last modification date: 2024-05-29) |
| Primary citation | Kwan, A.H.Y.,Gell, D.A.,Verger, A.,Crossley, M.,Matthews, J.M.,Mackay, J.P. Engineering a Protein Scaffold from a PHD Finger structure, 11:803-813, 2003 Cited by PubMed Abstract: The design of proteins with tailored functions remains a relatively elusive goal. Small size, a well-defined structure, and the ability to maintain structural integrity despite multiple mutations are all desirable properties for such designer proteins. Many zinc binding domains fit this description. We determined the structure of a PHD finger from the transcriptional cofactor Mi2beta and investigated the suitability of this domain as a scaffold for presenting selected binding functions. The two flexible loops in the structure were mutated extensively by either substitution or expansion, without affecting the overall fold of the domain. A binding site for the corepressor CtBP2 was also grafted onto the domain, creating a new PHD domain that can specifically bind CtBP2 both in vitro and in the context of a eukaryotic cell nucleus. These results represent a step toward designing new regulatory proteins for modulating aberrant gene expression in vivo. PubMed: 12842043DOI: 10.1016/S0969-2126(03)00122-9 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
