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p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept

1
Department of Molecular Medicine and USF Health Byrd Alzheimer’s Research Institute, Morsani College of Medicine, University of South Florida, 12901 Bruce B. Downs Blvd. MDC07, Tampa, FL 33612, USA
2
Laboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Sciences, 4 Tikhoretsky Ave., 194064 St. Petersburg, Russia
Academic Editor: Tomoo Iwakuma
Int. J. Mol. Sci. 2016, 17(11), 1874; https://doi.org/10.3390/ijms17111874
Received: 19 September 2016 / Revised: 27 October 2016 / Accepted: 3 November 2016 / Published: 10 November 2016
(This article belongs to the Special Issue Emerging Non-Canonical Functions and Regulation of p53)
Although it is one of the most studied proteins, p53 continues to be an enigma. This protein has numerous biological functions, possesses intrinsically disordered regions crucial for its functionality, can form both homo-tetramers and isoform-based hetero-tetramers, and is able to interact with many binding partners. It contains numerous posttranslational modifications, has several isoforms generated by alternative splicing, alternative promoter usage or alternative initiation of translation, and is commonly mutated in different cancers. Therefore, p53 serves as an important illustration of the protein structure–function continuum concept, where the generation of multiple proteoforms by various mechanisms defines the ability of this protein to have a multitude of structurally and functionally different states. Considering p53 in the light of a proteoform-based structure–function continuum represents a non-canonical and conceptually new contemplation of structure, regulation, and functionality of this important protein. View Full-Text
Keywords: p53; proteoform; protein structure–function continuum; cancer; mutation; posttranslational modification; intrinsically disordered protein; protein–protein interaction; alternative splicing p53; proteoform; protein structure–function continuum; cancer; mutation; posttranslational modification; intrinsically disordered protein; protein–protein interaction; alternative splicing
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MDPI and ACS Style

Uversky, V.N. p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept. Int. J. Mol. Sci. 2016, 17, 1874. https://doi.org/10.3390/ijms17111874

AMA Style

Uversky VN. p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept. International Journal of Molecular Sciences. 2016; 17(11):1874. https://doi.org/10.3390/ijms17111874

Chicago/Turabian Style

Uversky, Vladimir N. 2016. "p53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–Function Continuum Concept" Int. J. Mol. Sci. 17, no. 11: 1874. https://doi.org/10.3390/ijms17111874

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Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

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