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

By Vladimir N Uversky. 2016

164 citations recorded by the source corpus.

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.

Subfields: Materials Chemistry, Molecular Biology, Oncology

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Vladimir N Uversky

Citations in the corpus

SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning (2019, background): “IDPs are able to fulﬁl a wide range of niche, yet biologically crucial functional roles despite their lack of a rigid structure, due to their ability to transition between a set of transient, interconverting structural states [3].”
Intrinsic disorder here, there, and everywhere, and nowhere to escape from it (2017, background): “, due to the presence of IDPRs, posttranslational modifications, and isoforms created by alternative splicing, alternative promoter usage, or alternative initiation of translation, and induced as a result of function) characterized by a broad spectrum of structural features and possessing various fu”
Intrinsically Disordered Proteins and Their “Mysterious” (Meta)Physics (2019, background): “factors increasing chemical variability of a polypeptide chain, the protein structural diversity can be further increased by intrinsic disorder and functioning [93].”