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PDBsum entry 4d1m
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Transcription
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PDB id
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4d1m
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Contents |
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38 a.a.
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40 a.a.
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40 a.a.
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39 a.a.
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42 a.a.
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PDB id:
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Transcription
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Title:
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Tetramerization domain of zebrafish p53 (crystal form ii)
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Structure:
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Cellular tumor antigen p53. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Fragment: tetramerization domain, residues 302-346. Synonym: p53. Engineered: yes
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Source:
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Danio rerio. Zebrafish. Organism_taxid: 7955. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.20Å
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R-factor:
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0.228
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R-free:
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0.280
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Authors:
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A.C.Joerger
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Key ref:
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A.C.Joerger
et al.
(2014).
Tracing the evolution of the p53 tetramerization domain.
Structure,
22,
1301-1310.
PubMed id:
DOI:
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Date:
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02-May-14
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Release date:
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27-Aug-14
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PROCHECK
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Headers
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References
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G1K2L5
(G1K2L5_DANRE) -
Cellular tumor antigen p53 from Danio rerio
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Seq:
Struc:
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374 a.a.
38 a.a.
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G1K2L5
(G1K2L5_DANRE) -
Cellular tumor antigen p53 from Danio rerio
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Seq:
Struc:
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374 a.a.
40 a.a.
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G1K2L5
(G1K2L5_DANRE) -
Cellular tumor antigen p53 from Danio rerio
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Seq:
Struc:
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374 a.a.
40 a.a.
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K, L:
E.C.?
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DOI no:
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Structure
22:1301-1310
(2014)
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PubMed id:
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Tracing the evolution of the p53 tetramerization domain.
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A.C.Joerger,
R.Wilcken,
A.Andreeva.
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ABSTRACT
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The tetrameric transcription factors p53, p63, and p73 evolved from a common
ancestor and play key roles in tumor suppression and development. Surprisingly,
p63 and p73 require a second helix in their tetramerization domain for the
formation of stable tetramers that is absent in human p53, raising questions
about the evolutionary processes leading to diversification. Here we determined
the crystal structure of the zebrafish p53 tetramerization domain, which
contains a second helix, reminiscent of p63 and p73, combined with p53-like
features. Through comprehensive phylogenetic analyses, we systematically traced
the evolution of vertebrate p53 family oligomerization domains back to the
beginning of multicellular life. We provide evidence that their last common
ancestor also had an extended p63/p73-like domain and pinpoint evolutionary
events that shaped this domain during vertebrate radiation. Domain compaction
and transformation of a structured into a flexible, intrinsically disordered
region may have contributed to the expansion of the human p53 interactome.
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