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PDBsum entry 2mw4
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Transcription
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PDB id
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2mw4
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PDB id:
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| Name: |
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Transcription
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Title:
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Tetramerization domain of the ciona intestinalis p53/p73-b transcription factor protein
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Structure:
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Transcription factor protein. Chain: a, b, c, d. Fragment: tetramerization domain (unp residues 374-419). Engineered: yes
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Source:
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Ciona intestinalis. Sea vase,yellow sea squirt. Organism_taxid: 7719. Gene: ci-p53/p73-b. Expressed in: escherichia coli. Expression_system_taxid: 562.
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NMR struc:
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20 models
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Authors:
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J.P.Heering,H.R.A.Jonker,F.Loehr,H.Schwalbe,V.Doetsch
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Key ref:
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J.Heering
et al.
(2016).
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.
PubMed id:
DOI:
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Date:
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27-Oct-14
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Release date:
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28-Oct-15
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PROCHECK
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Headers
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References
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F6SSG7
(F6SSG7_CIOIN) -
Cellular tumor antigen p53 from Ciona intestinalis
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Seq:
Struc:
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419 a.a.
47 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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DOI no:
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Protein Sci
25:410-422
(2016)
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PubMed id:
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Structural investigations of the p53/p73 homologs from the tunicate species Ciona intestinalis reveal the sequence requirements for the formation of a tetramerization domain.
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J.Heering,
H.R.Jonker,
F.Löhr,
H.Schwalbe,
V.Dötsch.
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ABSTRACT
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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.
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Links
