Refined solution structure of the oligomerization domain of the tumour suppressor p53 (Q27730292)

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26 October 2019

title

Refined solution structure of the oligomerization domain of the tumour suppressor p53 (English)

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26 October 2019

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1

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26 October 2019

Angela Gronenborn

8

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26 October 2019

author name string

J Ernst

2

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26 October 2019

R Clubb

3

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26 October 2019

J G Omichinski

4

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26 October 2019

W M Kennedy

5

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26 October 2019

K Sakaguchi

6

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26 October 2019

E Appella

7

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26 October 2019

publication date

1 April 1995

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Nature Structural Biology

26 October 2019

language of work or name

English

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published in

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26 October 2019

volume

2

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26 October 2019

issue

4

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26 October 2019

page(s)

321-333

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Mutations in the p53 gene occur in diverse human tumour types

26 October 2019

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The DNA-binding domain of p53 contains the four conserved regions and the major mutation hot spots

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A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein

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Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

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High-resolution structure of the oligomerization domain of p53 by multidimensional NMR

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Solution structure of the tetrameric minimum transforming domain of p53

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Specific sequences from the carboxyl terminus of human p53 gene product form anti-parallel tetramers in solution

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Cotranslation of activated mutant p53 with wild type drives the wild-type p53 protein into the mutant conformation

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The dihedral symmetry of the p53 tetramerization domain mandates a conformational switch upon DNA binding

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inferred from DOI database lookup

7 January 2021

based on heuristic

Conformational shifts propagate from the oligomerization domain of p53 to its tetrameric DNA binding domain and restore DNA binding to select p53 mutants.

1 reference

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