2MW4
Tetramerization domain of the Ciona intestinalis p53/p73-b transcription factor protein
Summary for 2MW4
| Entry DOI | 10.2210/pdb2mw4/pdb |
| NMR Information | BMRB: 25298 |
| Descriptor | Transcription factor protein (1 entity in total) |
| Functional Keywords | ciona intestinalis, p53/p73-b, transcription factor, tetramerization domain, transcription |
| Biological source | Ciona intestinalis (sea vase,yellow sea squirt) |
| Total number of polymer chains | 4 |
| Total formula weight | 22113.46 |
| Authors | Heering, J.P.,Jonker, H.R.A.,Loehr, F.,Schwalbe, H.,Doetsch, V. (deposition date: 2014-10-27, release date: 2015-10-28, Last modification date: 2024-05-15) |
| Primary citation | Heering, J.,Jonker, H.R.,Lohr, F.,Schwalbe, H.,Dotsch, V. Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain. Protein Sci., 25:410-422, 2016 Cited by PubMed Abstract: Most members of the p53 family of transcription factors form tetramers. Responsible for determining the oligomeric state is a short oligomerization domain consisting of one β-strand and one α-helix. With the exception of human p53 all other family members investigated so far contain a second α-helix as part of their tetramerization domain. Here we have used nuclear magnetic resonance spectroscopy to characterize the oligomerization domains of the two p53-like proteins from the tunicate Ciona intestinalis, representing the closest living relative of vertebrates. Structure determination reveals for one of the two proteins a new type of packing of this second α-helix on the core domain that was not predicted based on the sequence, while the other protein does not form a second helix despite the presence of crucial residues that are conserved in all other family members that form a second helix. By mutational analysis, we identify a proline as well as large hydrophobic residues in the hinge region between both helices as the crucial determinant for the formation of a second helix. PubMed: 26473758DOI: 10.1002/pro.2830 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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