2MBH
NMR structure of EKLF(22-40)/Ubiquitin Complex
Summary for 2MBH
| Entry DOI | 10.2210/pdb2mbh/pdb |
| NMR Information | BMRB: 19399 |
| Descriptor | Krueppel-like factor 1, Ubiquitin (2 entities in total) |
| Functional Keywords | protein-protein complex, eklf, ubiquitin, uim/miu, transcription factor tad, transcription |
| Biological source | Homo sapiens (human) More |
| Cellular location | Nucleus: Q13351 |
| Total number of polymer chains | 2 |
| Total formula weight | 13020.64 |
| Authors | Raiola, L.,Omichinski, J.G. (deposition date: 2013-07-31, release date: 2013-10-09, Last modification date: 2024-05-15) |
| Primary citation | Raiola, L.,Lussier-Price, M.,Gagnon, D.,Lafrance-Vanasse, J.,Mascle, X.,Arseneault, G.,Legault, P.,Archambault, J.,Omichinski, J.G. Structural Characterization of a Noncovalent Complex between Ubiquitin and the Transactivation Domain of the Erythroid-Specific Factor EKLF. Structure, 21:2014-2024, 2013 Cited by PubMed Abstract: Like other acidic transactivation domains (TAD), the minimal TAD from the erythroid-specific transcription factor EKLF (EKLFTAD) has been shown to contribute both to its transcriptional activity as well as to its ubiquitin(UBI)-mediated degradation. In this article, we examine the activation-degradation role of the acidic TAD of EKLF and demonstrate that the first 40 residues (EKLFTAD1) within this region form a noncovalent interaction with UBI. Nuclear magnetic resonance (NMR) structural studies of an EKLFTAD1-UBI complex show that EKLFTAD1 adopts a 14-residue α helix that forms the recognition interface with UBI in a similar manner as the UBI-interacting helix of Rabex5. We also identify a similar interaction between UBI and the activation-degradation region of SREBP1a, but not with the activation-degradation regions of p53, GAL4, and VP16. These results suggest that select activation-degradation regions like the ones found in EKLF and SREBP1a function in part through their ability to form noncovalent interactions with UBI. PubMed: 24139988DOI: 10.1016/j.str.2013.08.027 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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