P53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–function Continuum Concept
Document Type
Article
Publication Date
2016
Keywords
P53, Proteoform, Protein Structure–function Continuum, Cancer, Mutation, Posttranslational Modification, Intrinsically Disordered Protein, Protein–protein Interaction, Alternative Splicing
Digital Object Identifier (DOI)
https://doi.org/10.3390/ijms17111874
Abstract
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.
Rights Information
This work is licensed under a Creative Commons Attribution 4.0 License.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
International Journal of Molecular Sciences, v. 17, issue 11, p. 1874
Scholar Commons Citation
Uversky, Vladimir N., "P53 Proteoforms and Intrinsic Disorder: An Illustration of the Protein Structure–function Continuum Concept" (2016). Molecular Medicine Faculty Publications. 865.
https://digitalcommons.usf.edu/mme_facpub/865
