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2KBY

The Tetramerization Domain of Human p73

Summary for 2KBY
Entry DOI10.2210/pdb2kby/pdb
DescriptorTumor protein p73 (1 entity in total)
Functional Keywordstetramerization domain, activator, alternative splicing, anti-oncogene, apoptosis, cell cycle, dna-binding, metal-binding, nucleus, phosphoprotein, transcription, transcription regulation, ubl conjugation, zinc
Biological sourceHomo sapiens (Human)
Cellular locationNucleus: O15350
Total number of polymer chains4
Total formula weight24139.31
Authors
Coutandin, D.,Ikeya, T.,Loehr, F.,Guntert, P.,Ou, H.D.,Doetsch, V. (deposition date: 2008-12-12, release date: 2009-09-29, Last modification date: 2024-05-29)
Primary citationCoutandin, D.,Lohr, F.,Niesen, F.H.,Ikeya, T.,Weber, T.A.,Schafer, B.,Zielonka, E.M.,Bullock, A.N.,Yang, A.,Guntert, P.,Knapp, S.,McKeon, F.,Ou, H.D.,Dotsch, V.
Conformational stability and activity of p73 require a second helix in the tetramerization domain.
Cell Death Differ., 16:1582-1589, 2009
Cited by
PubMed Abstract: p73 and p63, the two ancestral members of the p53 family, are involved in neurogenesis, epithelial stem cell maintenance and quality control of female germ cells. The highly conserved oligomerization domain (OD) of tumor suppressor p53 is essential for its biological functions, and its structure was believed to be the prototype for all three proteins. However, we report that the ODs of p73 and p63 differ from the OD of p53 by containing an additional alpha-helix that is not present in the structure of the p53 OD. Deletion of this helix causes a dissociation of the OD into dimers; it also causes conformational instability and reduces the transcriptional activity of p73. Moreover, we show that ODs of p73 and p63 strongly interact and that a large number of different heterotetramers are supported by the additional helix. Detailed analysis shows that the heterotetramer consisting of two homodimers is thermodynamically more stable than the two homotetramers. No heterooligomerization between p53 and the p73/p63 subfamily was observed, supporting the notion of functional orthogonality within the p53 family.
PubMed: 19763140
DOI: 10.1038/cdd.2009.139
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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