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Quantitative analysis of residual folding and DNA binding in mutant p53 core domain: definition of mutant states for rescue in cancer therapy.

Abstract:

The tumour suppressor p53 is mutated in half of all human cancers, most frequently with missense substitutions in its core domain. We present a new assessment of the mutation database based on quantitative folding and DNA-binding studies of the isolated core domain. Our data identify five distinct mutant classes that correlate with four well-defined regions of the core domain structure. On extrapolation to 37 degrees C the wild-type protein has a stability of 3.0 kcal/mol. This also emerges a...

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Publisher copy:
10.1038/sj.onc.1203434

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Genomics Consortium
Role:
Author
Journal:
Oncogene More from this journal
Volume:
19
Issue:
10
Pages:
1245-1256
Publication date:
2000-03-01
DOI:
EISSN:
1476-5594
ISSN:
0950-9232
Language:
English
Keywords:
Pubs id:
pubs:93030
UUID:
uuid:c8d1041d-913e-4b1f-a498-8d8aafd8adbd
Local pid:
pubs:93030
Source identifiers:
93030
Deposit date:
2013-02-20

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