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Interaction of the p53 DNA-binding domain with its n-terminal extension modulates the stability of the p53 tetramer.

Abstract:

The tetrameric tumor suppressor p53 plays a pivotal role in the control of the cell cycle and provides a paradigm for an emerging class of oligomeric, multidomain proteins with structured and intrinsically disordered regions. Many of its biophysical and functional properties have been extrapolated from truncated variants, yet the exact structural and functional role of certain segments of the protein is unclear. We found from NMR and X-ray crystallography that the DNA-binding domain (DBD) of ...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2011.03.047

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Journal:
Journal of molecular biology
Volume:
409
Issue:
3
Pages:
358-368
Publication date:
2011-06-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:9bf3a4a3-917c-485a-88dd-fb23587f606e
Source identifiers:
131081
Local pid:
pubs:131081

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