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Proteomics. 2015 Aug;15(16):2746-55. doi: 10.1002/pmic.201400549. Epub 2015 Apr 21.

Structure of full-length p53 tumor suppressor probed by chemical cross-linking and mass spectrometry.

Author information

1
Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, Halle (Saale), Germany.

Abstract

The tumor suppressor p53 presents a great challenge for 3D structural analysis due to its inherent flexibility. In this work, we gained insight into the structure of full-length wild-type human p53 in solution by chemical cross-linking/MS. This approach allowed us obtaining structural information of free wild-type p53 in solution without making use of the ultrastable quadruple p53 variant. The cross-links within one p53 monomer are in good agreement with the small-angle X-ray scattering based model of full-length p53. Our cross-linking data between different p53 molecules in the tetramer however indicate a large degree of flexibility in the C-terminal regulatory domain of full-length p53 in the absence of DNA. The cross-links suggest that the C-terminal regulatory domains are much closer to each other, resulting in a more compact arrangement of the p53 tetramer than perceived by the small-angle X-ray scattering model.

KEYWORDS:

3D structure; Chemical cross-linking; Intrinsically disordered proteins; MS; Technology; p53

PMID:
25728495
DOI:
10.1002/pmic.201400549
[Indexed for MEDLINE]

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