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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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J.Heering,
H.R.Jonker,
F.Löhr,
H.Schwalbe,
V.Dötsch.
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Ref.
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Protein Sci, 2016,
25,
410-422.
[DOI no: ]
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PubMed id
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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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